data_9EP2
# 
_entry.id   9EP2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EP2         pdb_00009ep2 10.2210/pdb9ep2/pdb 
WWPDB D_1292137362 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EP2 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              andrea.angeli@unifi.it 
_pdbx_contact_author.name_first         Andrea 
_pdbx_contact_author.name_last          Angeli 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1470-7192 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Angeli, A.'    1 0000-0002-1470-7192 
'Ferraroni, M.' 2 0000-0001-7258-738X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of the complex of human carbonic anhydrase I with 4-sulfamoylphenyl 3-(p-tolylthio)propanoate' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Angeli, A.'    1 0000-0002-1470-7192 
primary 'Ferraroni, M.' 2 0000-0001-7258-738X 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 1'                                     28906.186 2   4.2.1.1 ? ? ? 
2 non-polymer syn 'ACETATE ION'                                              59.044    2   ?       ? ? ? 
3 non-polymer syn 'ZINC ION'                                                 65.409    2   ?       ? ? ? 
4 non-polymer syn '(4-sulfamoylphenyl) 3-(4-methylphenyl)sulfanylpropanoate' 351.440   2   ?       ? ? ? 
5 water       nat water                                                      18.015    442 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase I,Carbonic anhydrase B,CAB,Carbonic anhydrase I,CA-I' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVL
KGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQK
VLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAV
PMQHNNRPTQPLKGRTVRASF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVL
KGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQK
VLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAV
PMQHNNRPTQPLKGRTVRASF
;
_entity_poly.pdbx_strand_id                 AAA,BBB 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ACETATE ION'                                              ACT   
3 'ZINC ION'                                                 ZN    
4 '(4-sulfamoylphenyl) 3-(4-methylphenyl)sulfanylpropanoate' A1H6C 
5 water                                                      HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   SER n 
1 4   PRO n 
1 5   ASP n 
1 6   TRP n 
1 7   GLY n 
1 8   TYR n 
1 9   ASP n 
1 10  ASP n 
1 11  LYS n 
1 12  ASN n 
1 13  GLY n 
1 14  PRO n 
1 15  GLU n 
1 16  GLN n 
1 17  TRP n 
1 18  SER n 
1 19  LYS n 
1 20  LEU n 
1 21  TYR n 
1 22  PRO n 
1 23  ILE n 
1 24  ALA n 
1 25  ASN n 
1 26  GLY n 
1 27  ASN n 
1 28  ASN n 
1 29  GLN n 
1 30  SER n 
1 31  PRO n 
1 32  VAL n 
1 33  ASP n 
1 34  ILE n 
1 35  LYS n 
1 36  THR n 
1 37  SER n 
1 38  GLU n 
1 39  THR n 
1 40  LYS n 
1 41  HIS n 
1 42  ASP n 
1 43  THR n 
1 44  SER n 
1 45  LEU n 
1 46  LYS n 
1 47  PRO n 
1 48  ILE n 
1 49  SER n 
1 50  VAL n 
1 51  SER n 
1 52  TYR n 
1 53  ASN n 
1 54  PRO n 
1 55  ALA n 
1 56  THR n 
1 57  ALA n 
1 58  LYS n 
1 59  GLU n 
1 60  ILE n 
1 61  ILE n 
1 62  ASN n 
1 63  VAL n 
1 64  GLY n 
1 65  HIS n 
1 66  SER n 
1 67  PHE n 
1 68  HIS n 
1 69  VAL n 
1 70  ASN n 
1 71  PHE n 
1 72  GLU n 
1 73  ASP n 
1 74  ASN n 
1 75  ASP n 
1 76  ASN n 
1 77  ARG n 
1 78  SER n 
1 79  VAL n 
1 80  LEU n 
1 81  LYS n 
1 82  GLY n 
1 83  GLY n 
1 84  PRO n 
1 85  PHE n 
1 86  SER n 
1 87  ASP n 
1 88  SER n 
1 89  TYR n 
1 90  ARG n 
1 91  LEU n 
1 92  PHE n 
1 93  GLN n 
1 94  PHE n 
1 95  HIS n 
1 96  PHE n 
1 97  HIS n 
1 98  TRP n 
1 99  GLY n 
1 100 SER n 
1 101 THR n 
1 102 ASN n 
1 103 GLU n 
1 104 HIS n 
1 105 GLY n 
1 106 SER n 
1 107 GLU n 
1 108 HIS n 
1 109 THR n 
1 110 VAL n 
1 111 ASP n 
1 112 GLY n 
1 113 VAL n 
1 114 LYS n 
1 115 TYR n 
1 116 SER n 
1 117 ALA n 
1 118 GLU n 
1 119 LEU n 
1 120 HIS n 
1 121 VAL n 
1 122 ALA n 
1 123 HIS n 
1 124 TRP n 
1 125 ASN n 
1 126 SER n 
1 127 ALA n 
1 128 LYS n 
1 129 TYR n 
1 130 SER n 
1 131 SER n 
1 132 LEU n 
1 133 ALA n 
1 134 GLU n 
1 135 ALA n 
1 136 ALA n 
1 137 SER n 
1 138 LYS n 
1 139 ALA n 
1 140 ASP n 
1 141 GLY n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 ILE n 
1 146 GLY n 
1 147 VAL n 
1 148 LEU n 
1 149 MET n 
1 150 LYS n 
1 151 VAL n 
1 152 GLY n 
1 153 GLU n 
1 154 ALA n 
1 155 ASN n 
1 156 PRO n 
1 157 LYS n 
1 158 LEU n 
1 159 GLN n 
1 160 LYS n 
1 161 VAL n 
1 162 LEU n 
1 163 ASP n 
1 164 ALA n 
1 165 LEU n 
1 166 GLN n 
1 167 ALA n 
1 168 ILE n 
1 169 LYS n 
1 170 THR n 
1 171 LYS n 
1 172 GLY n 
1 173 LYS n 
1 174 ARG n 
1 175 ALA n 
1 176 PRO n 
1 177 PHE n 
1 178 THR n 
1 179 ASN n 
1 180 PHE n 
1 181 ASP n 
1 182 PRO n 
1 183 SER n 
1 184 THR n 
1 185 LEU n 
1 186 LEU n 
1 187 PRO n 
1 188 SER n 
1 189 SER n 
1 190 LEU n 
1 191 ASP n 
1 192 PHE n 
1 193 TRP n 
1 194 THR n 
1 195 TYR n 
1 196 PRO n 
1 197 GLY n 
1 198 SER n 
1 199 LEU n 
1 200 THR n 
1 201 HIS n 
1 202 PRO n 
1 203 PRO n 
1 204 LEU n 
1 205 TYR n 
1 206 GLU n 
1 207 SER n 
1 208 VAL n 
1 209 THR n 
1 210 TRP n 
1 211 ILE n 
1 212 ILE n 
1 213 CYS n 
1 214 LYS n 
1 215 GLU n 
1 216 SER n 
1 217 ILE n 
1 218 SER n 
1 219 VAL n 
1 220 SER n 
1 221 SER n 
1 222 GLU n 
1 223 GLN n 
1 224 LEU n 
1 225 ALA n 
1 226 GLN n 
1 227 PHE n 
1 228 ARG n 
1 229 SER n 
1 230 LEU n 
1 231 LEU n 
1 232 SER n 
1 233 ASN n 
1 234 VAL n 
1 235 GLU n 
1 236 GLY n 
1 237 ASP n 
1 238 ASN n 
1 239 ALA n 
1 240 VAL n 
1 241 PRO n 
1 242 MET n 
1 243 GLN n 
1 244 HIS n 
1 245 ASN n 
1 246 ASN n 
1 247 ARG n 
1 248 PRO n 
1 249 THR n 
1 250 GLN n 
1 251 PRO n 
1 252 LEU n 
1 253 LYS n 
1 254 GLY n 
1 255 ARG n 
1 256 THR n 
1 257 VAL n 
1 258 ARG n 
1 259 ALA n 
1 260 SER n 
1 261 PHE n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   261 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1H6C non-polymer         . '(4-sulfamoylphenyl) 3-(4-methylphenyl)sulfanylpropanoate' 
'4-sulfamoylphenyl 3-(p-tolylthio)propanoate' 'C16 H17 N O4 S2' 351.440 
ACT   non-polymer         . 'ACETATE ION'                                              ? 'C2 H3 O2 -1'     59.044  
ALA   'L-peptide linking' y ALANINE                                                    ? 'C3 H7 N O2'      89.093  
ARG   'L-peptide linking' y ARGININE                                                   ? 'C6 H15 N4 O2 1'  175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                 ? 'C4 H8 N2 O3'     132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                            ? 'C4 H7 N O4'      133.103 
CYS   'L-peptide linking' y CYSTEINE                                                   ? 'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                  ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                            ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE                                                    ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE                                                  ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER                                                      ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                 ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE                                                    ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE                                                     ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE                                                 ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                              ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE                                                    ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE                                                     ? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE                                                  ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                 ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE                                                   ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE                                                     ? 'C5 H11 N O2'     117.146 
ZN    non-polymer         . 'ZINC ION'                                                 ? 'Zn 2'            65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   AAA . n 
A 1 2   ALA 2   1   ?   ?   ?   AAA . n 
A 1 3   SER 3   2   ?   ?   ?   AAA . n 
A 1 4   PRO 4   3   ?   ?   ?   AAA . n 
A 1 5   ASP 5   4   4   ASP ASP AAA . n 
A 1 6   TRP 6   5   5   TRP TRP AAA . n 
A 1 7   GLY 7   6   6   GLY GLY AAA . n 
A 1 8   TYR 8   7   7   TYR TYR AAA . n 
A 1 9   ASP 9   8   8   ASP ASP AAA . n 
A 1 10  ASP 10  9   9   ASP ASP AAA . n 
A 1 11  LYS 11  10  10  LYS LYS AAA . n 
A 1 12  ASN 12  11  11  ASN ASN AAA . n 
A 1 13  GLY 13  12  12  GLY GLY AAA . n 
A 1 14  PRO 14  13  13  PRO PRO AAA . n 
A 1 15  GLU 15  14  14  GLU GLU AAA . n 
A 1 16  GLN 16  15  15  GLN GLN AAA . n 
A 1 17  TRP 17  16  16  TRP TRP AAA . n 
A 1 18  SER 18  17  17  SER SER AAA . n 
A 1 19  LYS 19  18  18  LYS LYS AAA . n 
A 1 20  LEU 20  19  19  LEU LEU AAA . n 
A 1 21  TYR 21  20  20  TYR TYR AAA . n 
A 1 22  PRO 22  21  21  PRO PRO AAA . n 
A 1 23  ILE 23  22  22  ILE ILE AAA . n 
A 1 24  ALA 24  23  23  ALA ALA AAA . n 
A 1 25  ASN 25  24  24  ASN ASN AAA . n 
A 1 26  GLY 26  25  25  GLY GLY AAA . n 
A 1 27  ASN 27  26  26  ASN ASN AAA . n 
A 1 28  ASN 28  27  27  ASN ASN AAA . n 
A 1 29  GLN 29  28  28  GLN GLN AAA . n 
A 1 30  SER 30  29  29  SER SER AAA . n 
A 1 31  PRO 31  30  30  PRO PRO AAA . n 
A 1 32  VAL 32  31  31  VAL VAL AAA . n 
A 1 33  ASP 33  32  32  ASP ASP AAA . n 
A 1 34  ILE 34  33  33  ILE ILE AAA . n 
A 1 35  LYS 35  34  34  LYS LYS AAA . n 
A 1 36  THR 36  35  35  THR THR AAA . n 
A 1 37  SER 37  36  36  SER SER AAA . n 
A 1 38  GLU 38  37  37  GLU GLU AAA . n 
A 1 39  THR 39  38  38  THR THR AAA . n 
A 1 40  LYS 40  39  39  LYS LYS AAA . n 
A 1 41  HIS 41  40  40  HIS HIS AAA . n 
A 1 42  ASP 42  41  41  ASP ASP AAA . n 
A 1 43  THR 43  42  42  THR THR AAA . n 
A 1 44  SER 44  43  43  SER SER AAA . n 
A 1 45  LEU 45  44  44  LEU LEU AAA . n 
A 1 46  LYS 46  45  45  LYS LYS AAA . n 
A 1 47  PRO 47  46  46  PRO PRO AAA . n 
A 1 48  ILE 48  47  47  ILE ILE AAA . n 
A 1 49  SER 49  48  48  SER SER AAA . n 
A 1 50  VAL 50  49  49  VAL VAL AAA . n 
A 1 51  SER 51  50  50  SER SER AAA . n 
A 1 52  TYR 52  51  51  TYR TYR AAA . n 
A 1 53  ASN 53  52  52  ASN ASN AAA . n 
A 1 54  PRO 54  53  53  PRO PRO AAA . n 
A 1 55  ALA 55  54  54  ALA ALA AAA . n 
A 1 56  THR 56  55  55  THR THR AAA . n 
A 1 57  ALA 57  56  56  ALA ALA AAA . n 
A 1 58  LYS 58  57  57  LYS LYS AAA . n 
A 1 59  GLU 59  58  58  GLU GLU AAA . n 
A 1 60  ILE 60  59  59  ILE ILE AAA . n 
A 1 61  ILE 61  60  60  ILE ILE AAA . n 
A 1 62  ASN 62  61  61  ASN ASN AAA . n 
A 1 63  VAL 63  62  62  VAL VAL AAA . n 
A 1 64  GLY 64  63  63  GLY GLY AAA . n 
A 1 65  HIS 65  64  64  HIS HIS AAA . n 
A 1 66  SER 66  65  65  SER SER AAA . n 
A 1 67  PHE 67  66  66  PHE PHE AAA . n 
A 1 68  HIS 68  67  67  HIS HIS AAA . n 
A 1 69  VAL 69  68  68  VAL VAL AAA . n 
A 1 70  ASN 70  69  69  ASN ASN AAA . n 
A 1 71  PHE 71  70  70  PHE PHE AAA . n 
A 1 72  GLU 72  71  71  GLU GLU AAA . n 
A 1 73  ASP 73  72  72  ASP ASP AAA . n 
A 1 74  ASN 74  73  73  ASN ASN AAA . n 
A 1 75  ASP 75  74  74  ASP ASP AAA . n 
A 1 76  ASN 76  75  75  ASN ASN AAA . n 
A 1 77  ARG 77  76  76  ARG ARG AAA . n 
A 1 78  SER 78  77  77  SER SER AAA . n 
A 1 79  VAL 79  78  78  VAL VAL AAA . n 
A 1 80  LEU 80  79  79  LEU LEU AAA . n 
A 1 81  LYS 81  80  80  LYS LYS AAA . n 
A 1 82  GLY 82  81  81  GLY GLY AAA . n 
A 1 83  GLY 83  82  82  GLY GLY AAA . n 
A 1 84  PRO 84  83  83  PRO PRO AAA . n 
A 1 85  PHE 85  84  84  PHE PHE AAA . n 
A 1 86  SER 86  85  85  SER SER AAA . n 
A 1 87  ASP 87  86  86  ASP ASP AAA . n 
A 1 88  SER 88  87  87  SER SER AAA . n 
A 1 89  TYR 89  88  88  TYR TYR AAA . n 
A 1 90  ARG 90  89  89  ARG ARG AAA . n 
A 1 91  LEU 91  90  90  LEU LEU AAA . n 
A 1 92  PHE 92  91  91  PHE PHE AAA . n 
A 1 93  GLN 93  92  92  GLN GLN AAA . n 
A 1 94  PHE 94  93  93  PHE PHE AAA . n 
A 1 95  HIS 95  94  94  HIS HIS AAA . n 
A 1 96  PHE 96  95  95  PHE PHE AAA . n 
A 1 97  HIS 97  96  96  HIS HIS AAA . n 
A 1 98  TRP 98  97  97  TRP TRP AAA . n 
A 1 99  GLY 99  98  98  GLY GLY AAA . n 
A 1 100 SER 100 99  99  SER SER AAA . n 
A 1 101 THR 101 100 100 THR THR AAA . n 
A 1 102 ASN 102 101 101 ASN ASN AAA . n 
A 1 103 GLU 103 102 102 GLU GLU AAA . n 
A 1 104 HIS 104 103 103 HIS HIS AAA . n 
A 1 105 GLY 105 104 104 GLY GLY AAA . n 
A 1 106 SER 106 105 105 SER SER AAA . n 
A 1 107 GLU 107 106 106 GLU GLU AAA . n 
A 1 108 HIS 108 107 107 HIS HIS AAA . n 
A 1 109 THR 109 108 108 THR THR AAA . n 
A 1 110 VAL 110 109 109 VAL VAL AAA . n 
A 1 111 ASP 111 110 110 ASP ASP AAA . n 
A 1 112 GLY 112 111 111 GLY GLY AAA . n 
A 1 113 VAL 113 112 112 VAL VAL AAA . n 
A 1 114 LYS 114 113 113 LYS LYS AAA . n 
A 1 115 TYR 115 114 114 TYR TYR AAA . n 
A 1 116 SER 116 115 115 SER SER AAA . n 
A 1 117 ALA 117 116 116 ALA ALA AAA . n 
A 1 118 GLU 118 117 117 GLU GLU AAA . n 
A 1 119 LEU 119 118 118 LEU LEU AAA . n 
A 1 120 HIS 120 119 119 HIS HIS AAA . n 
A 1 121 VAL 121 120 120 VAL VAL AAA . n 
A 1 122 ALA 122 121 121 ALA ALA AAA . n 
A 1 123 HIS 123 122 122 HIS HIS AAA . n 
A 1 124 TRP 124 123 123 TRP TRP AAA . n 
A 1 125 ASN 125 124 124 ASN ASN AAA . n 
A 1 126 SER 126 125 125 SER SER AAA . n 
A 1 127 ALA 127 126 126 ALA ALA AAA . n 
A 1 128 LYS 128 127 127 LYS LYS AAA . n 
A 1 129 TYR 129 128 128 TYR TYR AAA . n 
A 1 130 SER 130 129 129 SER SER AAA . n 
A 1 131 SER 131 130 130 SER SER AAA . n 
A 1 132 LEU 132 131 131 LEU LEU AAA . n 
A 1 133 ALA 133 132 132 ALA ALA AAA . n 
A 1 134 GLU 134 133 133 GLU GLU AAA . n 
A 1 135 ALA 135 134 134 ALA ALA AAA . n 
A 1 136 ALA 136 135 135 ALA ALA AAA . n 
A 1 137 SER 137 136 136 SER SER AAA . n 
A 1 138 LYS 138 137 137 LYS LYS AAA . n 
A 1 139 ALA 139 138 138 ALA ALA AAA . n 
A 1 140 ASP 140 139 139 ASP ASP AAA . n 
A 1 141 GLY 141 140 140 GLY GLY AAA . n 
A 1 142 LEU 142 141 141 LEU LEU AAA . n 
A 1 143 ALA 143 142 142 ALA ALA AAA . n 
A 1 144 VAL 144 143 143 VAL VAL AAA . n 
A 1 145 ILE 145 144 144 ILE ILE AAA . n 
A 1 146 GLY 146 145 145 GLY GLY AAA . n 
A 1 147 VAL 147 146 146 VAL VAL AAA . n 
A 1 148 LEU 148 147 147 LEU LEU AAA . n 
A 1 149 MET 149 148 148 MET MET AAA . n 
A 1 150 LYS 150 149 149 LYS LYS AAA . n 
A 1 151 VAL 151 150 150 VAL VAL AAA . n 
A 1 152 GLY 152 151 151 GLY GLY AAA . n 
A 1 153 GLU 153 152 152 GLU GLU AAA . n 
A 1 154 ALA 154 153 153 ALA ALA AAA . n 
A 1 155 ASN 155 154 154 ASN ASN AAA . n 
A 1 156 PRO 156 155 155 PRO PRO AAA . n 
A 1 157 LYS 157 156 156 LYS LYS AAA . n 
A 1 158 LEU 158 157 157 LEU LEU AAA . n 
A 1 159 GLN 159 158 158 GLN GLN AAA . n 
A 1 160 LYS 160 159 159 LYS LYS AAA . n 
A 1 161 VAL 161 160 160 VAL VAL AAA . n 
A 1 162 LEU 162 161 161 LEU LEU AAA . n 
A 1 163 ASP 163 162 162 ASP ASP AAA . n 
A 1 164 ALA 164 163 163 ALA ALA AAA . n 
A 1 165 LEU 165 164 164 LEU LEU AAA . n 
A 1 166 GLN 166 165 165 GLN GLN AAA . n 
A 1 167 ALA 167 166 166 ALA ALA AAA . n 
A 1 168 ILE 168 167 167 ILE ILE AAA . n 
A 1 169 LYS 169 168 168 LYS LYS AAA . n 
A 1 170 THR 170 169 169 THR THR AAA . n 
A 1 171 LYS 171 170 170 LYS LYS AAA . n 
A 1 172 GLY 172 171 171 GLY GLY AAA . n 
A 1 173 LYS 173 172 172 LYS LYS AAA . n 
A 1 174 ARG 174 173 173 ARG ARG AAA . n 
A 1 175 ALA 175 174 174 ALA ALA AAA . n 
A 1 176 PRO 176 175 175 PRO PRO AAA . n 
A 1 177 PHE 177 176 176 PHE PHE AAA . n 
A 1 178 THR 178 177 177 THR THR AAA . n 
A 1 179 ASN 179 178 178 ASN ASN AAA . n 
A 1 180 PHE 180 179 179 PHE PHE AAA . n 
A 1 181 ASP 181 180 180 ASP ASP AAA . n 
A 1 182 PRO 182 181 181 PRO PRO AAA . n 
A 1 183 SER 183 182 182 SER SER AAA . n 
A 1 184 THR 184 183 183 THR THR AAA . n 
A 1 185 LEU 185 184 184 LEU LEU AAA . n 
A 1 186 LEU 186 185 185 LEU LEU AAA . n 
A 1 187 PRO 187 186 186 PRO PRO AAA . n 
A 1 188 SER 188 187 187 SER SER AAA . n 
A 1 189 SER 189 188 188 SER SER AAA . n 
A 1 190 LEU 190 189 189 LEU LEU AAA . n 
A 1 191 ASP 191 190 190 ASP ASP AAA . n 
A 1 192 PHE 192 191 191 PHE PHE AAA . n 
A 1 193 TRP 193 192 192 TRP TRP AAA . n 
A 1 194 THR 194 193 193 THR THR AAA . n 
A 1 195 TYR 195 194 194 TYR TYR AAA . n 
A 1 196 PRO 196 195 195 PRO PRO AAA . n 
A 1 197 GLY 197 196 196 GLY GLY AAA . n 
A 1 198 SER 198 197 197 SER SER AAA . n 
A 1 199 LEU 199 198 198 LEU LEU AAA . n 
A 1 200 THR 200 199 199 THR THR AAA . n 
A 1 201 HIS 201 200 200 HIS HIS AAA . n 
A 1 202 PRO 202 201 201 PRO PRO AAA . n 
A 1 203 PRO 203 202 202 PRO PRO AAA . n 
A 1 204 LEU 204 203 203 LEU LEU AAA . n 
A 1 205 TYR 205 204 204 TYR TYR AAA . n 
A 1 206 GLU 206 205 205 GLU GLU AAA . n 
A 1 207 SER 207 206 206 SER SER AAA . n 
A 1 208 VAL 208 207 207 VAL VAL AAA . n 
A 1 209 THR 209 208 208 THR THR AAA . n 
A 1 210 TRP 210 209 209 TRP TRP AAA . n 
A 1 211 ILE 211 210 210 ILE ILE AAA . n 
A 1 212 ILE 212 211 211 ILE ILE AAA . n 
A 1 213 CYS 213 212 212 CYS CYS AAA . n 
A 1 214 LYS 214 213 213 LYS LYS AAA . n 
A 1 215 GLU 215 214 214 GLU GLU AAA . n 
A 1 216 SER 216 215 215 SER SER AAA . n 
A 1 217 ILE 217 216 216 ILE ILE AAA . n 
A 1 218 SER 218 217 217 SER SER AAA . n 
A 1 219 VAL 219 218 218 VAL VAL AAA . n 
A 1 220 SER 220 219 219 SER SER AAA . n 
A 1 221 SER 221 220 220 SER SER AAA . n 
A 1 222 GLU 222 221 221 GLU GLU AAA . n 
A 1 223 GLN 223 222 222 GLN GLN AAA . n 
A 1 224 LEU 224 223 223 LEU LEU AAA . n 
A 1 225 ALA 225 224 224 ALA ALA AAA . n 
A 1 226 GLN 226 225 225 GLN GLN AAA . n 
A 1 227 PHE 227 226 226 PHE PHE AAA . n 
A 1 228 ARG 228 227 227 ARG ARG AAA . n 
A 1 229 SER 229 228 228 SER SER AAA . n 
A 1 230 LEU 230 229 229 LEU LEU AAA . n 
A 1 231 LEU 231 230 230 LEU LEU AAA . n 
A 1 232 SER 232 231 231 SER SER AAA . n 
A 1 233 ASN 233 232 232 ASN ASN AAA . n 
A 1 234 VAL 234 233 233 VAL VAL AAA . n 
A 1 235 GLU 235 234 234 GLU GLU AAA . n 
A 1 236 GLY 236 235 235 GLY GLY AAA . n 
A 1 237 ASP 237 236 236 ASP ASP AAA . n 
A 1 238 ASN 238 237 237 ASN ASN AAA . n 
A 1 239 ALA 239 238 238 ALA ALA AAA . n 
A 1 240 VAL 240 239 239 VAL VAL AAA . n 
A 1 241 PRO 241 240 240 PRO PRO AAA . n 
A 1 242 MET 242 241 241 MET MET AAA . n 
A 1 243 GLN 243 242 242 GLN GLN AAA . n 
A 1 244 HIS 244 243 243 HIS HIS AAA . n 
A 1 245 ASN 245 244 244 ASN ASN AAA . n 
A 1 246 ASN 246 245 245 ASN ASN AAA . n 
A 1 247 ARG 247 246 246 ARG ARG AAA . n 
A 1 248 PRO 248 247 247 PRO PRO AAA . n 
A 1 249 THR 249 248 248 THR THR AAA . n 
A 1 250 GLN 250 249 249 GLN GLN AAA . n 
A 1 251 PRO 251 250 250 PRO PRO AAA . n 
A 1 252 LEU 252 251 251 LEU LEU AAA . n 
A 1 253 LYS 253 252 252 LYS LYS AAA . n 
A 1 254 GLY 254 253 253 GLY GLY AAA . n 
A 1 255 ARG 255 254 254 ARG ARG AAA . n 
A 1 256 THR 256 255 255 THR THR AAA . n 
A 1 257 VAL 257 256 256 VAL VAL AAA . n 
A 1 258 ARG 258 257 257 ARG ARG AAA . n 
A 1 259 ALA 259 258 258 ALA ALA AAA . n 
A 1 260 SER 260 259 259 SER SER AAA . n 
A 1 261 PHE 261 260 260 PHE PHE AAA . n 
B 1 1   MET 1   0   ?   ?   ?   BBB . n 
B 1 2   ALA 2   1   ?   ?   ?   BBB . n 
B 1 3   SER 3   2   2   SER SER BBB . n 
B 1 4   PRO 4   3   3   PRO PRO BBB . n 
B 1 5   ASP 5   4   4   ASP ASP BBB . n 
B 1 6   TRP 6   5   5   TRP TRP BBB . n 
B 1 7   GLY 7   6   6   GLY GLY BBB . n 
B 1 8   TYR 8   7   7   TYR TYR BBB . n 
B 1 9   ASP 9   8   8   ASP ASP BBB . n 
B 1 10  ASP 10  9   9   ASP ASP BBB . n 
B 1 11  LYS 11  10  10  LYS LYS BBB . n 
B 1 12  ASN 12  11  11  ASN ASN BBB . n 
B 1 13  GLY 13  12  12  GLY GLY BBB . n 
B 1 14  PRO 14  13  13  PRO PRO BBB . n 
B 1 15  GLU 15  14  14  GLU GLU BBB . n 
B 1 16  GLN 16  15  15  GLN GLN BBB . n 
B 1 17  TRP 17  16  16  TRP TRP BBB . n 
B 1 18  SER 18  17  17  SER SER BBB . n 
B 1 19  LYS 19  18  18  LYS LYS BBB . n 
B 1 20  LEU 20  19  19  LEU LEU BBB . n 
B 1 21  TYR 21  20  20  TYR TYR BBB . n 
B 1 22  PRO 22  21  21  PRO PRO BBB . n 
B 1 23  ILE 23  22  22  ILE ILE BBB . n 
B 1 24  ALA 24  23  23  ALA ALA BBB . n 
B 1 25  ASN 25  24  24  ASN ASN BBB . n 
B 1 26  GLY 26  25  25  GLY GLY BBB . n 
B 1 27  ASN 27  26  26  ASN ASN BBB . n 
B 1 28  ASN 28  27  27  ASN ASN BBB . n 
B 1 29  GLN 29  28  28  GLN GLN BBB . n 
B 1 30  SER 30  29  29  SER SER BBB . n 
B 1 31  PRO 31  30  30  PRO PRO BBB . n 
B 1 32  VAL 32  31  31  VAL VAL BBB . n 
B 1 33  ASP 33  32  32  ASP ASP BBB . n 
B 1 34  ILE 34  33  33  ILE ILE BBB . n 
B 1 35  LYS 35  34  34  LYS LYS BBB . n 
B 1 36  THR 36  35  35  THR THR BBB . n 
B 1 37  SER 37  36  36  SER SER BBB . n 
B 1 38  GLU 38  37  37  GLU GLU BBB . n 
B 1 39  THR 39  38  38  THR THR BBB . n 
B 1 40  LYS 40  39  39  LYS LYS BBB . n 
B 1 41  HIS 41  40  40  HIS HIS BBB . n 
B 1 42  ASP 42  41  41  ASP ASP BBB . n 
B 1 43  THR 43  42  42  THR THR BBB . n 
B 1 44  SER 44  43  43  SER SER BBB . n 
B 1 45  LEU 45  44  44  LEU LEU BBB . n 
B 1 46  LYS 46  45  45  LYS LYS BBB . n 
B 1 47  PRO 47  46  46  PRO PRO BBB . n 
B 1 48  ILE 48  47  47  ILE ILE BBB . n 
B 1 49  SER 49  48  48  SER SER BBB . n 
B 1 50  VAL 50  49  49  VAL VAL BBB . n 
B 1 51  SER 51  50  50  SER SER BBB . n 
B 1 52  TYR 52  51  51  TYR TYR BBB . n 
B 1 53  ASN 53  52  52  ASN ASN BBB . n 
B 1 54  PRO 54  53  53  PRO PRO BBB . n 
B 1 55  ALA 55  54  54  ALA ALA BBB . n 
B 1 56  THR 56  55  55  THR THR BBB . n 
B 1 57  ALA 57  56  56  ALA ALA BBB . n 
B 1 58  LYS 58  57  57  LYS LYS BBB . n 
B 1 59  GLU 59  58  58  GLU GLU BBB . n 
B 1 60  ILE 60  59  59  ILE ILE BBB . n 
B 1 61  ILE 61  60  60  ILE ILE BBB . n 
B 1 62  ASN 62  61  61  ASN ASN BBB . n 
B 1 63  VAL 63  62  62  VAL VAL BBB . n 
B 1 64  GLY 64  63  63  GLY GLY BBB . n 
B 1 65  HIS 65  64  64  HIS HIS BBB . n 
B 1 66  SER 66  65  65  SER SER BBB . n 
B 1 67  PHE 67  66  66  PHE PHE BBB . n 
B 1 68  HIS 68  67  67  HIS HIS BBB . n 
B 1 69  VAL 69  68  68  VAL VAL BBB . n 
B 1 70  ASN 70  69  69  ASN ASN BBB . n 
B 1 71  PHE 71  70  70  PHE PHE BBB . n 
B 1 72  GLU 72  71  71  GLU GLU BBB . n 
B 1 73  ASP 73  72  72  ASP ASP BBB . n 
B 1 74  ASN 74  73  73  ASN ASN BBB . n 
B 1 75  ASP 75  74  74  ASP ASP BBB . n 
B 1 76  ASN 76  75  75  ASN ASN BBB . n 
B 1 77  ARG 77  76  76  ARG ARG BBB . n 
B 1 78  SER 78  77  77  SER SER BBB . n 
B 1 79  VAL 79  78  78  VAL VAL BBB . n 
B 1 80  LEU 80  79  79  LEU LEU BBB . n 
B 1 81  LYS 81  80  80  LYS LYS BBB . n 
B 1 82  GLY 82  81  81  GLY GLY BBB . n 
B 1 83  GLY 83  82  82  GLY GLY BBB . n 
B 1 84  PRO 84  83  83  PRO PRO BBB . n 
B 1 85  PHE 85  84  84  PHE PHE BBB . n 
B 1 86  SER 86  85  85  SER SER BBB . n 
B 1 87  ASP 87  86  86  ASP ASP BBB . n 
B 1 88  SER 88  87  87  SER SER BBB . n 
B 1 89  TYR 89  88  88  TYR TYR BBB . n 
B 1 90  ARG 90  89  89  ARG ARG BBB . n 
B 1 91  LEU 91  90  90  LEU LEU BBB . n 
B 1 92  PHE 92  91  91  PHE PHE BBB . n 
B 1 93  GLN 93  92  92  GLN GLN BBB . n 
B 1 94  PHE 94  93  93  PHE PHE BBB . n 
B 1 95  HIS 95  94  94  HIS HIS BBB . n 
B 1 96  PHE 96  95  95  PHE PHE BBB . n 
B 1 97  HIS 97  96  96  HIS HIS BBB . n 
B 1 98  TRP 98  97  97  TRP TRP BBB . n 
B 1 99  GLY 99  98  98  GLY GLY BBB . n 
B 1 100 SER 100 99  99  SER SER BBB . n 
B 1 101 THR 101 100 100 THR THR BBB . n 
B 1 102 ASN 102 101 101 ASN ASN BBB . n 
B 1 103 GLU 103 102 102 GLU GLU BBB . n 
B 1 104 HIS 104 103 103 HIS HIS BBB . n 
B 1 105 GLY 105 104 104 GLY GLY BBB . n 
B 1 106 SER 106 105 105 SER SER BBB . n 
B 1 107 GLU 107 106 106 GLU GLU BBB . n 
B 1 108 HIS 108 107 107 HIS HIS BBB . n 
B 1 109 THR 109 108 108 THR THR BBB . n 
B 1 110 VAL 110 109 109 VAL VAL BBB . n 
B 1 111 ASP 111 110 110 ASP ASP BBB . n 
B 1 112 GLY 112 111 111 GLY GLY BBB . n 
B 1 113 VAL 113 112 112 VAL VAL BBB . n 
B 1 114 LYS 114 113 113 LYS LYS BBB . n 
B 1 115 TYR 115 114 114 TYR TYR BBB . n 
B 1 116 SER 116 115 115 SER SER BBB . n 
B 1 117 ALA 117 116 116 ALA ALA BBB . n 
B 1 118 GLU 118 117 117 GLU GLU BBB . n 
B 1 119 LEU 119 118 118 LEU LEU BBB . n 
B 1 120 HIS 120 119 119 HIS HIS BBB . n 
B 1 121 VAL 121 120 120 VAL VAL BBB . n 
B 1 122 ALA 122 121 121 ALA ALA BBB . n 
B 1 123 HIS 123 122 122 HIS HIS BBB . n 
B 1 124 TRP 124 123 123 TRP TRP BBB . n 
B 1 125 ASN 125 124 124 ASN ASN BBB . n 
B 1 126 SER 126 125 125 SER SER BBB . n 
B 1 127 ALA 127 126 126 ALA ALA BBB . n 
B 1 128 LYS 128 127 127 LYS LYS BBB . n 
B 1 129 TYR 129 128 128 TYR TYR BBB . n 
B 1 130 SER 130 129 129 SER SER BBB . n 
B 1 131 SER 131 130 130 SER SER BBB . n 
B 1 132 LEU 132 131 131 LEU LEU BBB . n 
B 1 133 ALA 133 132 132 ALA ALA BBB . n 
B 1 134 GLU 134 133 133 GLU GLU BBB . n 
B 1 135 ALA 135 134 134 ALA ALA BBB . n 
B 1 136 ALA 136 135 135 ALA ALA BBB . n 
B 1 137 SER 137 136 136 SER SER BBB . n 
B 1 138 LYS 138 137 137 LYS LYS BBB . n 
B 1 139 ALA 139 138 138 ALA ALA BBB . n 
B 1 140 ASP 140 139 139 ASP ASP BBB . n 
B 1 141 GLY 141 140 140 GLY GLY BBB . n 
B 1 142 LEU 142 141 141 LEU LEU BBB . n 
B 1 143 ALA 143 142 142 ALA ALA BBB . n 
B 1 144 VAL 144 143 143 VAL VAL BBB . n 
B 1 145 ILE 145 144 144 ILE ILE BBB . n 
B 1 146 GLY 146 145 145 GLY GLY BBB . n 
B 1 147 VAL 147 146 146 VAL VAL BBB . n 
B 1 148 LEU 148 147 147 LEU LEU BBB . n 
B 1 149 MET 149 148 148 MET MET BBB . n 
B 1 150 LYS 150 149 149 LYS LYS BBB . n 
B 1 151 VAL 151 150 150 VAL VAL BBB . n 
B 1 152 GLY 152 151 151 GLY GLY BBB . n 
B 1 153 GLU 153 152 152 GLU GLU BBB . n 
B 1 154 ALA 154 153 153 ALA ALA BBB . n 
B 1 155 ASN 155 154 154 ASN ASN BBB . n 
B 1 156 PRO 156 155 155 PRO PRO BBB . n 
B 1 157 LYS 157 156 156 LYS LYS BBB . n 
B 1 158 LEU 158 157 157 LEU LEU BBB . n 
B 1 159 GLN 159 158 158 GLN GLN BBB . n 
B 1 160 LYS 160 159 159 LYS LYS BBB . n 
B 1 161 VAL 161 160 160 VAL VAL BBB . n 
B 1 162 LEU 162 161 161 LEU LEU BBB . n 
B 1 163 ASP 163 162 162 ASP ASP BBB . n 
B 1 164 ALA 164 163 163 ALA ALA BBB . n 
B 1 165 LEU 165 164 164 LEU LEU BBB . n 
B 1 166 GLN 166 165 165 GLN GLN BBB . n 
B 1 167 ALA 167 166 166 ALA ALA BBB . n 
B 1 168 ILE 168 167 167 ILE ILE BBB . n 
B 1 169 LYS 169 168 168 LYS LYS BBB . n 
B 1 170 THR 170 169 169 THR THR BBB . n 
B 1 171 LYS 171 170 170 LYS LYS BBB . n 
B 1 172 GLY 172 171 171 GLY GLY BBB . n 
B 1 173 LYS 173 172 172 LYS LYS BBB . n 
B 1 174 ARG 174 173 173 ARG ARG BBB . n 
B 1 175 ALA 175 174 174 ALA ALA BBB . n 
B 1 176 PRO 176 175 175 PRO PRO BBB . n 
B 1 177 PHE 177 176 176 PHE PHE BBB . n 
B 1 178 THR 178 177 177 THR THR BBB . n 
B 1 179 ASN 179 178 178 ASN ASN BBB . n 
B 1 180 PHE 180 179 179 PHE PHE BBB . n 
B 1 181 ASP 181 180 180 ASP ASP BBB . n 
B 1 182 PRO 182 181 181 PRO PRO BBB . n 
B 1 183 SER 183 182 182 SER SER BBB . n 
B 1 184 THR 184 183 183 THR THR BBB . n 
B 1 185 LEU 185 184 184 LEU LEU BBB . n 
B 1 186 LEU 186 185 185 LEU LEU BBB . n 
B 1 187 PRO 187 186 186 PRO PRO BBB . n 
B 1 188 SER 188 187 187 SER SER BBB . n 
B 1 189 SER 189 188 188 SER SER BBB . n 
B 1 190 LEU 190 189 189 LEU LEU BBB . n 
B 1 191 ASP 191 190 190 ASP ASP BBB . n 
B 1 192 PHE 192 191 191 PHE PHE BBB . n 
B 1 193 TRP 193 192 192 TRP TRP BBB . n 
B 1 194 THR 194 193 193 THR THR BBB . n 
B 1 195 TYR 195 194 194 TYR TYR BBB . n 
B 1 196 PRO 196 195 195 PRO PRO BBB . n 
B 1 197 GLY 197 196 196 GLY GLY BBB . n 
B 1 198 SER 198 197 197 SER SER BBB . n 
B 1 199 LEU 199 198 198 LEU LEU BBB . n 
B 1 200 THR 200 199 199 THR THR BBB . n 
B 1 201 HIS 201 200 200 HIS HIS BBB . n 
B 1 202 PRO 202 201 201 PRO PRO BBB . n 
B 1 203 PRO 203 202 202 PRO PRO BBB . n 
B 1 204 LEU 204 203 203 LEU LEU BBB . n 
B 1 205 TYR 205 204 204 TYR TYR BBB . n 
B 1 206 GLU 206 205 205 GLU GLU BBB . n 
B 1 207 SER 207 206 206 SER SER BBB . n 
B 1 208 VAL 208 207 207 VAL VAL BBB . n 
B 1 209 THR 209 208 208 THR THR BBB . n 
B 1 210 TRP 210 209 209 TRP TRP BBB . n 
B 1 211 ILE 211 210 210 ILE ILE BBB . n 
B 1 212 ILE 212 211 211 ILE ILE BBB . n 
B 1 213 CYS 213 212 212 CYS CYS BBB . n 
B 1 214 LYS 214 213 213 LYS LYS BBB . n 
B 1 215 GLU 215 214 214 GLU GLU BBB . n 
B 1 216 SER 216 215 215 SER SER BBB . n 
B 1 217 ILE 217 216 216 ILE ILE BBB . n 
B 1 218 SER 218 217 217 SER SER BBB . n 
B 1 219 VAL 219 218 218 VAL VAL BBB . n 
B 1 220 SER 220 219 219 SER SER BBB . n 
B 1 221 SER 221 220 220 SER SER BBB . n 
B 1 222 GLU 222 221 221 GLU GLU BBB . n 
B 1 223 GLN 223 222 222 GLN GLN BBB . n 
B 1 224 LEU 224 223 223 LEU LEU BBB . n 
B 1 225 ALA 225 224 224 ALA ALA BBB . n 
B 1 226 GLN 226 225 225 GLN GLN BBB . n 
B 1 227 PHE 227 226 226 PHE PHE BBB . n 
B 1 228 ARG 228 227 227 ARG ARG BBB . n 
B 1 229 SER 229 228 228 SER SER BBB . n 
B 1 230 LEU 230 229 229 LEU LEU BBB . n 
B 1 231 LEU 231 230 230 LEU LEU BBB . n 
B 1 232 SER 232 231 231 SER SER BBB . n 
B 1 233 ASN 233 232 232 ASN ASN BBB . n 
B 1 234 VAL 234 233 233 VAL VAL BBB . n 
B 1 235 GLU 235 234 234 GLU GLU BBB . n 
B 1 236 GLY 236 235 235 GLY GLY BBB . n 
B 1 237 ASP 237 236 236 ASP ASP BBB . n 
B 1 238 ASN 238 237 237 ASN ASN BBB . n 
B 1 239 ALA 239 238 238 ALA ALA BBB . n 
B 1 240 VAL 240 239 239 VAL VAL BBB . n 
B 1 241 PRO 241 240 240 PRO PRO BBB . n 
B 1 242 MET 242 241 241 MET MET BBB . n 
B 1 243 GLN 243 242 242 GLN GLN BBB . n 
B 1 244 HIS 244 243 243 HIS HIS BBB . n 
B 1 245 ASN 245 244 244 ASN ASN BBB . n 
B 1 246 ASN 246 245 245 ASN ASN BBB . n 
B 1 247 ARG 247 246 246 ARG ARG BBB . n 
B 1 248 PRO 248 247 247 PRO PRO BBB . n 
B 1 249 THR 249 248 248 THR THR BBB . n 
B 1 250 GLN 250 249 249 GLN GLN BBB . n 
B 1 251 PRO 251 250 250 PRO PRO BBB . n 
B 1 252 LEU 252 251 251 LEU LEU BBB . n 
B 1 253 LYS 253 252 252 LYS LYS BBB . n 
B 1 254 GLY 254 253 253 GLY GLY BBB . n 
B 1 255 ARG 255 254 254 ARG ARG BBB . n 
B 1 256 THR 256 255 255 THR THR BBB . n 
B 1 257 VAL 257 256 256 VAL VAL BBB . n 
B 1 258 ARG 258 257 257 ARG ARG BBB . n 
B 1 259 ALA 259 258 258 ALA ALA BBB . n 
B 1 260 SER 260 259 259 SER SER BBB . n 
B 1 261 PHE 261 260 260 PHE PHE BBB . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H6C 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H6C 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ACT   1   301 302 ACT   ACT AAA . 
D 2 ACT   1   302 303 ACT   ACT AAA . 
E 3 ZN    1   303 261 ZN    ZN  AAA . 
F 4 A1H6C 1   304 300 A1H6C AOX AAA . 
G 3 ZN    1   301 1   ZN    ZN  BBB . 
H 4 A1H6C 1   302 301 A1H6C AOX BBB . 
I 5 HOH   1   401 401 HOH   HOH AAA . 
I 5 HOH   2   402 448 HOH   HOH AAA . 
I 5 HOH   3   403 428 HOH   HOH AAA . 
I 5 HOH   4   404 205 HOH   HOH AAA . 
I 5 HOH   5   405 384 HOH   HOH AAA . 
I 5 HOH   6   406 396 HOH   HOH AAA . 
I 5 HOH   7   407 418 HOH   HOH AAA . 
I 5 HOH   8   408 434 HOH   HOH AAA . 
I 5 HOH   9   409 150 HOH   HOH AAA . 
I 5 HOH   10  410 363 HOH   HOH AAA . 
I 5 HOH   11  411 61  HOH   HOH AAA . 
I 5 HOH   12  412 33  HOH   HOH AAA . 
I 5 HOH   13  413 228 HOH   HOH AAA . 
I 5 HOH   14  414 13  HOH   HOH AAA . 
I 5 HOH   15  415 247 HOH   HOH AAA . 
I 5 HOH   16  416 235 HOH   HOH AAA . 
I 5 HOH   17  417 372 HOH   HOH AAA . 
I 5 HOH   18  418 216 HOH   HOH AAA . 
I 5 HOH   19  419 275 HOH   HOH AAA . 
I 5 HOH   20  420 316 HOH   HOH AAA . 
I 5 HOH   21  421 319 HOH   HOH AAA . 
I 5 HOH   22  422 326 HOH   HOH AAA . 
I 5 HOH   23  423 62  HOH   HOH AAA . 
I 5 HOH   24  424 424 HOH   HOH AAA . 
I 5 HOH   25  425 391 HOH   HOH AAA . 
I 5 HOH   26  426 176 HOH   HOH AAA . 
I 5 HOH   27  427 92  HOH   HOH AAA . 
I 5 HOH   28  428 218 HOH   HOH AAA . 
I 5 HOH   29  429 144 HOH   HOH AAA . 
I 5 HOH   30  430 43  HOH   HOH AAA . 
I 5 HOH   31  431 145 HOH   HOH AAA . 
I 5 HOH   32  432 123 HOH   HOH AAA . 
I 5 HOH   33  433 63  HOH   HOH AAA . 
I 5 HOH   34  434 139 HOH   HOH AAA . 
I 5 HOH   35  435 50  HOH   HOH AAA . 
I 5 HOH   36  436 239 HOH   HOH AAA . 
I 5 HOH   37  437 153 HOH   HOH AAA . 
I 5 HOH   38  438 301 HOH   HOH AAA . 
I 5 HOH   39  439 233 HOH   HOH AAA . 
I 5 HOH   40  440 427 HOH   HOH AAA . 
I 5 HOH   41  441 361 HOH   HOH AAA . 
I 5 HOH   42  442 126 HOH   HOH AAA . 
I 5 HOH   43  443 217 HOH   HOH AAA . 
I 5 HOH   44  444 97  HOH   HOH AAA . 
I 5 HOH   45  445 231 HOH   HOH AAA . 
I 5 HOH   46  446 303 HOH   HOH AAA . 
I 5 HOH   47  447 32  HOH   HOH AAA . 
I 5 HOH   48  448 289 HOH   HOH AAA . 
I 5 HOH   49  449 69  HOH   HOH AAA . 
I 5 HOH   50  450 287 HOH   HOH AAA . 
I 5 HOH   51  451 60  HOH   HOH AAA . 
I 5 HOH   52  452 166 HOH   HOH AAA . 
I 5 HOH   53  453 197 HOH   HOH AAA . 
I 5 HOH   54  454 328 HOH   HOH AAA . 
I 5 HOH   55  455 122 HOH   HOH AAA . 
I 5 HOH   56  456 132 HOH   HOH AAA . 
I 5 HOH   57  457 113 HOH   HOH AAA . 
I 5 HOH   58  458 175 HOH   HOH AAA . 
I 5 HOH   59  459 35  HOH   HOH AAA . 
I 5 HOH   60  460 295 HOH   HOH AAA . 
I 5 HOH   61  461 26  HOH   HOH AAA . 
I 5 HOH   62  462 196 HOH   HOH AAA . 
I 5 HOH   63  463 412 HOH   HOH AAA . 
I 5 HOH   64  464 31  HOH   HOH AAA . 
I 5 HOH   65  465 131 HOH   HOH AAA . 
I 5 HOH   66  466 147 HOH   HOH AAA . 
I 5 HOH   67  467 98  HOH   HOH AAA . 
I 5 HOH   68  468 154 HOH   HOH AAA . 
I 5 HOH   69  469 29  HOH   HOH AAA . 
I 5 HOH   70  470 109 HOH   HOH AAA . 
I 5 HOH   71  471 195 HOH   HOH AAA . 
I 5 HOH   72  472 48  HOH   HOH AAA . 
I 5 HOH   73  473 55  HOH   HOH AAA . 
I 5 HOH   74  474 206 HOH   HOH AAA . 
I 5 HOH   75  475 190 HOH   HOH AAA . 
I 5 HOH   76  476 19  HOH   HOH AAA . 
I 5 HOH   77  477 5   HOH   HOH AAA . 
I 5 HOH   78  478 265 HOH   HOH AAA . 
I 5 HOH   79  479 317 HOH   HOH AAA . 
I 5 HOH   80  480 21  HOH   HOH AAA . 
I 5 HOH   81  481 96  HOH   HOH AAA . 
I 5 HOH   82  482 8   HOH   HOH AAA . 
I 5 HOH   83  483 3   HOH   HOH AAA . 
I 5 HOH   84  484 394 HOH   HOH AAA . 
I 5 HOH   85  485 75  HOH   HOH AAA . 
I 5 HOH   86  486 107 HOH   HOH AAA . 
I 5 HOH   87  487 236 HOH   HOH AAA . 
I 5 HOH   88  488 58  HOH   HOH AAA . 
I 5 HOH   89  489 181 HOH   HOH AAA . 
I 5 HOH   90  490 334 HOH   HOH AAA . 
I 5 HOH   91  491 49  HOH   HOH AAA . 
I 5 HOH   92  492 76  HOH   HOH AAA . 
I 5 HOH   93  493 450 HOH   HOH AAA . 
I 5 HOH   94  494 99  HOH   HOH AAA . 
I 5 HOH   95  495 259 HOH   HOH AAA . 
I 5 HOH   96  496 291 HOH   HOH AAA . 
I 5 HOH   97  497 57  HOH   HOH AAA . 
I 5 HOH   98  498 121 HOH   HOH AAA . 
I 5 HOH   99  499 194 HOH   HOH AAA . 
I 5 HOH   100 500 325 HOH   HOH AAA . 
I 5 HOH   101 501 232 HOH   HOH AAA . 
I 5 HOH   102 502 66  HOH   HOH AAA . 
I 5 HOH   103 503 117 HOH   HOH AAA . 
I 5 HOH   104 504 198 HOH   HOH AAA . 
I 5 HOH   105 505 191 HOH   HOH AAA . 
I 5 HOH   106 506 395 HOH   HOH AAA . 
I 5 HOH   107 507 120 HOH   HOH AAA . 
I 5 HOH   108 508 277 HOH   HOH AAA . 
I 5 HOH   109 509 7   HOH   HOH AAA . 
I 5 HOH   110 510 88  HOH   HOH AAA . 
I 5 HOH   111 511 420 HOH   HOH AAA . 
I 5 HOH   112 512 215 HOH   HOH AAA . 
I 5 HOH   113 513 330 HOH   HOH AAA . 
I 5 HOH   114 514 74  HOH   HOH AAA . 
I 5 HOH   115 515 404 HOH   HOH AAA . 
I 5 HOH   116 516 115 HOH   HOH AAA . 
I 5 HOH   117 517 146 HOH   HOH AAA . 
I 5 HOH   118 518 152 HOH   HOH AAA . 
I 5 HOH   119 519 182 HOH   HOH AAA . 
I 5 HOH   120 520 156 HOH   HOH AAA . 
I 5 HOH   121 521 369 HOH   HOH AAA . 
I 5 HOH   122 522 253 HOH   HOH AAA . 
I 5 HOH   123 523 81  HOH   HOH AAA . 
I 5 HOH   124 524 349 HOH   HOH AAA . 
I 5 HOH   125 525 30  HOH   HOH AAA . 
I 5 HOH   126 526 204 HOH   HOH AAA . 
I 5 HOH   127 527 187 HOH   HOH AAA . 
I 5 HOH   128 528 39  HOH   HOH AAA . 
I 5 HOH   129 529 162 HOH   HOH AAA . 
I 5 HOH   130 530 167 HOH   HOH AAA . 
I 5 HOH   131 531 306 HOH   HOH AAA . 
I 5 HOH   132 532 381 HOH   HOH AAA . 
I 5 HOH   133 533 245 HOH   HOH AAA . 
I 5 HOH   134 534 244 HOH   HOH AAA . 
I 5 HOH   135 535 86  HOH   HOH AAA . 
I 5 HOH   136 536 125 HOH   HOH AAA . 
I 5 HOH   137 537 304 HOH   HOH AAA . 
I 5 HOH   138 538 161 HOH   HOH AAA . 
I 5 HOH   139 539 136 HOH   HOH AAA . 
I 5 HOH   140 540 65  HOH   HOH AAA . 
I 5 HOH   141 541 38  HOH   HOH AAA . 
I 5 HOH   142 542 134 HOH   HOH AAA . 
I 5 HOH   143 543 116 HOH   HOH AAA . 
I 5 HOH   144 544 20  HOH   HOH AAA . 
I 5 HOH   145 545 222 HOH   HOH AAA . 
I 5 HOH   146 546 23  HOH   HOH AAA . 
I 5 HOH   147 547 40  HOH   HOH AAA . 
I 5 HOH   148 548 432 HOH   HOH AAA . 
I 5 HOH   149 549 308 HOH   HOH AAA . 
I 5 HOH   150 550 174 HOH   HOH AAA . 
I 5 HOH   151 551 93  HOH   HOH AAA . 
I 5 HOH   152 552 286 HOH   HOH AAA . 
I 5 HOH   153 553 155 HOH   HOH AAA . 
I 5 HOH   154 554 445 HOH   HOH AAA . 
I 5 HOH   155 555 179 HOH   HOH AAA . 
I 5 HOH   156 556 263 HOH   HOH AAA . 
I 5 HOH   157 557 67  HOH   HOH AAA . 
I 5 HOH   158 558 371 HOH   HOH AAA . 
I 5 HOH   159 559 375 HOH   HOH AAA . 
I 5 HOH   160 560 417 HOH   HOH AAA . 
I 5 HOH   161 561 238 HOH   HOH AAA . 
I 5 HOH   162 562 271 HOH   HOH AAA . 
I 5 HOH   163 563 435 HOH   HOH AAA . 
I 5 HOH   164 564 393 HOH   HOH AAA . 
I 5 HOH   165 565 305 HOH   HOH AAA . 
I 5 HOH   166 566 421 HOH   HOH AAA . 
I 5 HOH   167 567 248 HOH   HOH AAA . 
I 5 HOH   168 568 169 HOH   HOH AAA . 
I 5 HOH   169 569 352 HOH   HOH AAA . 
I 5 HOH   170 570 178 HOH   HOH AAA . 
I 5 HOH   171 571 341 HOH   HOH AAA . 
I 5 HOH   172 572 82  HOH   HOH AAA . 
I 5 HOH   173 573 47  HOH   HOH AAA . 
I 5 HOH   174 574 436 HOH   HOH AAA . 
I 5 HOH   175 575 299 HOH   HOH AAA . 
I 5 HOH   176 576 399 HOH   HOH AAA . 
I 5 HOH   177 577 374 HOH   HOH AAA . 
I 5 HOH   178 578 200 HOH   HOH AAA . 
I 5 HOH   179 579 260 HOH   HOH AAA . 
I 5 HOH   180 580 209 HOH   HOH AAA . 
I 5 HOH   181 581 313 HOH   HOH AAA . 
I 5 HOH   182 582 419 HOH   HOH AAA . 
I 5 HOH   183 583 413 HOH   HOH AAA . 
I 5 HOH   184 584 297 HOH   HOH AAA . 
I 5 HOH   185 585 356 HOH   HOH AAA . 
I 5 HOH   186 586 118 HOH   HOH AAA . 
I 5 HOH   187 587 192 HOH   HOH AAA . 
I 5 HOH   188 588 437 HOH   HOH AAA . 
I 5 HOH   189 589 452 HOH   HOH AAA . 
I 5 HOH   190 590 423 HOH   HOH AAA . 
I 5 HOH   191 591 344 HOH   HOH AAA . 
I 5 HOH   192 592 298 HOH   HOH AAA . 
I 5 HOH   193 593 440 HOH   HOH AAA . 
I 5 HOH   194 594 188 HOH   HOH AAA . 
I 5 HOH   195 595 340 HOH   HOH AAA . 
I 5 HOH   196 596 438 HOH   HOH AAA . 
I 5 HOH   197 597 171 HOH   HOH AAA . 
I 5 HOH   198 598 314 HOH   HOH AAA . 
I 5 HOH   199 599 276 HOH   HOH AAA . 
I 5 HOH   200 600 342 HOH   HOH AAA . 
I 5 HOH   201 601 255 HOH   HOH AAA . 
I 5 HOH   202 602 346 HOH   HOH AAA . 
I 5 HOH   203 603 256 HOH   HOH AAA . 
I 5 HOH   204 604 425 HOH   HOH AAA . 
I 5 HOH   205 605 219 HOH   HOH AAA . 
I 5 HOH   206 606 141 HOH   HOH AAA . 
I 5 HOH   207 607 203 HOH   HOH AAA . 
I 5 HOH   208 608 225 HOH   HOH AAA . 
I 5 HOH   209 609 112 HOH   HOH AAA . 
I 5 HOH   210 610 444 HOH   HOH AAA . 
I 5 HOH   211 611 408 HOH   HOH AAA . 
I 5 HOH   212 612 431 HOH   HOH AAA . 
I 5 HOH   213 613 281 HOH   HOH AAA . 
I 5 HOH   214 614 279 HOH   HOH AAA . 
I 5 HOH   215 615 173 HOH   HOH AAA . 
I 5 HOH   216 616 202 HOH   HOH AAA . 
I 5 HOH   217 617 409 HOH   HOH AAA . 
I 5 HOH   218 618 354 HOH   HOH AAA . 
I 5 HOH   219 619 350 HOH   HOH AAA . 
J 5 HOH   1   401 398 HOH   HOH BBB . 
J 5 HOH   2   402 397 HOH   HOH BBB . 
J 5 HOH   3   403 380 HOH   HOH BBB . 
J 5 HOH   4   404 288 HOH   HOH BBB . 
J 5 HOH   5   405 193 HOH   HOH BBB . 
J 5 HOH   6   406 357 HOH   HOH BBB . 
J 5 HOH   7   407 211 HOH   HOH BBB . 
J 5 HOH   8   408 390 HOH   HOH BBB . 
J 5 HOH   9   409 358 HOH   HOH BBB . 
J 5 HOH   10  410 261 HOH   HOH BBB . 
J 5 HOH   11  411 362 HOH   HOH BBB . 
J 5 HOH   12  412 183 HOH   HOH BBB . 
J 5 HOH   13  413 407 HOH   HOH BBB . 
J 5 HOH   14  414 414 HOH   HOH BBB . 
J 5 HOH   15  415 229 HOH   HOH BBB . 
J 5 HOH   16  416 157 HOH   HOH BBB . 
J 5 HOH   17  417 243 HOH   HOH BBB . 
J 5 HOH   18  418 4   HOH   HOH BBB . 
J 5 HOH   19  419 377 HOH   HOH BBB . 
J 5 HOH   20  420 392 HOH   HOH BBB . 
J 5 HOH   21  421 104 HOH   HOH BBB . 
J 5 HOH   22  422 453 HOH   HOH BBB . 
J 5 HOH   23  423 451 HOH   HOH BBB . 
J 5 HOH   24  424 382 HOH   HOH BBB . 
J 5 HOH   25  425 415 HOH   HOH BBB . 
J 5 HOH   26  426 443 HOH   HOH BBB . 
J 5 HOH   27  427 70  HOH   HOH BBB . 
J 5 HOH   28  428 44  HOH   HOH BBB . 
J 5 HOH   29  429 186 HOH   HOH BBB . 
J 5 HOH   30  430 207 HOH   HOH BBB . 
J 5 HOH   31  431 249 HOH   HOH BBB . 
J 5 HOH   32  432 42  HOH   HOH BBB . 
J 5 HOH   33  433 108 HOH   HOH BBB . 
J 5 HOH   34  434 383 HOH   HOH BBB . 
J 5 HOH   35  435 365 HOH   HOH BBB . 
J 5 HOH   36  436 177 HOH   HOH BBB . 
J 5 HOH   37  437 378 HOH   HOH BBB . 
J 5 HOH   38  438 135 HOH   HOH BBB . 
J 5 HOH   39  439 364 HOH   HOH BBB . 
J 5 HOH   40  440 262 HOH   HOH BBB . 
J 5 HOH   41  441 283 HOH   HOH BBB . 
J 5 HOH   42  442 309 HOH   HOH BBB . 
J 5 HOH   43  443 449 HOH   HOH BBB . 
J 5 HOH   44  444 199 HOH   HOH BBB . 
J 5 HOH   45  445 170 HOH   HOH BBB . 
J 5 HOH   46  446 290 HOH   HOH BBB . 
J 5 HOH   47  447 11  HOH   HOH BBB . 
J 5 HOH   48  448 379 HOH   HOH BBB . 
J 5 HOH   49  449 447 HOH   HOH BBB . 
J 5 HOH   50  450 292 HOH   HOH BBB . 
J 5 HOH   51  451 52  HOH   HOH BBB . 
J 5 HOH   52  452 257 HOH   HOH BBB . 
J 5 HOH   53  453 37  HOH   HOH BBB . 
J 5 HOH   54  454 172 HOH   HOH BBB . 
J 5 HOH   55  455 143 HOH   HOH BBB . 
J 5 HOH   56  456 24  HOH   HOH BBB . 
J 5 HOH   57  457 51  HOH   HOH BBB . 
J 5 HOH   58  458 280 HOH   HOH BBB . 
J 5 HOH   59  459 168 HOH   HOH BBB . 
J 5 HOH   60  460 251 HOH   HOH BBB . 
J 5 HOH   61  461 94  HOH   HOH BBB . 
J 5 HOH   62  462 56  HOH   HOH BBB . 
J 5 HOH   63  463 250 HOH   HOH BBB . 
J 5 HOH   64  464 221 HOH   HOH BBB . 
J 5 HOH   65  465 83  HOH   HOH BBB . 
J 5 HOH   66  466 389 HOH   HOH BBB . 
J 5 HOH   67  467 15  HOH   HOH BBB . 
J 5 HOH   68  468 201 HOH   HOH BBB . 
J 5 HOH   69  469 128 HOH   HOH BBB . 
J 5 HOH   70  470 114 HOH   HOH BBB . 
J 5 HOH   71  471 2   HOH   HOH BBB . 
J 5 HOH   72  472 46  HOH   HOH BBB . 
J 5 HOH   73  473 180 HOH   HOH BBB . 
J 5 HOH   74  474 101 HOH   HOH BBB . 
J 5 HOH   75  475 110 HOH   HOH BBB . 
J 5 HOH   76  476 85  HOH   HOH BBB . 
J 5 HOH   77  477 148 HOH   HOH BBB . 
J 5 HOH   78  478 315 HOH   HOH BBB . 
J 5 HOH   79  479 158 HOH   HOH BBB . 
J 5 HOH   80  480 129 HOH   HOH BBB . 
J 5 HOH   81  481 127 HOH   HOH BBB . 
J 5 HOH   82  482 230 HOH   HOH BBB . 
J 5 HOH   83  483 28  HOH   HOH BBB . 
J 5 HOH   84  484 310 HOH   HOH BBB . 
J 5 HOH   85  485 267 HOH   HOH BBB . 
J 5 HOH   86  486 138 HOH   HOH BBB . 
J 5 HOH   87  487 237 HOH   HOH BBB . 
J 5 HOH   88  488 234 HOH   HOH BBB . 
J 5 HOH   89  489 73  HOH   HOH BBB . 
J 5 HOH   90  490 27  HOH   HOH BBB . 
J 5 HOH   91  491 71  HOH   HOH BBB . 
J 5 HOH   92  492 64  HOH   HOH BBB . 
J 5 HOH   93  493 72  HOH   HOH BBB . 
J 5 HOH   94  494 429 HOH   HOH BBB . 
J 5 HOH   95  495 254 HOH   HOH BBB . 
J 5 HOH   96  496 25  HOH   HOH BBB . 
J 5 HOH   97  497 321 HOH   HOH BBB . 
J 5 HOH   98  498 184 HOH   HOH BBB . 
J 5 HOH   99  499 272 HOH   HOH BBB . 
J 5 HOH   100 500 105 HOH   HOH BBB . 
J 5 HOH   101 501 273 HOH   HOH BBB . 
J 5 HOH   102 502 212 HOH   HOH BBB . 
J 5 HOH   103 503 89  HOH   HOH BBB . 
J 5 HOH   104 504 1   HOH   HOH BBB . 
J 5 HOH   105 505 77  HOH   HOH BBB . 
J 5 HOH   106 506 240 HOH   HOH BBB . 
J 5 HOH   107 507 214 HOH   HOH BBB . 
J 5 HOH   108 508 87  HOH   HOH BBB . 
J 5 HOH   109 509 269 HOH   HOH BBB . 
J 5 HOH   110 510 293 HOH   HOH BBB . 
J 5 HOH   111 511 80  HOH   HOH BBB . 
J 5 HOH   112 512 102 HOH   HOH BBB . 
J 5 HOH   113 513 18  HOH   HOH BBB . 
J 5 HOH   114 514 22  HOH   HOH BBB . 
J 5 HOH   115 515 266 HOH   HOH BBB . 
J 5 HOH   116 516 160 HOH   HOH BBB . 
J 5 HOH   117 517 210 HOH   HOH BBB . 
J 5 HOH   118 518 124 HOH   HOH BBB . 
J 5 HOH   119 519 149 HOH   HOH BBB . 
J 5 HOH   120 520 164 HOH   HOH BBB . 
J 5 HOH   121 521 12  HOH   HOH BBB . 
J 5 HOH   122 522 159 HOH   HOH BBB . 
J 5 HOH   123 523 227 HOH   HOH BBB . 
J 5 HOH   124 524 91  HOH   HOH BBB . 
J 5 HOH   125 525 95  HOH   HOH BBB . 
J 5 HOH   126 526 320 HOH   HOH BBB . 
J 5 HOH   127 527 208 HOH   HOH BBB . 
J 5 HOH   128 528 258 HOH   HOH BBB . 
J 5 HOH   129 529 130 HOH   HOH BBB . 
J 5 HOH   130 530 45  HOH   HOH BBB . 
J 5 HOH   131 531 400 HOH   HOH BBB . 
J 5 HOH   132 532 111 HOH   HOH BBB . 
J 5 HOH   133 533 165 HOH   HOH BBB . 
J 5 HOH   134 534 333 HOH   HOH BBB . 
J 5 HOH   135 535 252 HOH   HOH BBB . 
J 5 HOH   136 536 17  HOH   HOH BBB . 
J 5 HOH   137 537 264 HOH   HOH BBB . 
J 5 HOH   138 538 302 HOH   HOH BBB . 
J 5 HOH   139 539 36  HOH   HOH BBB . 
J 5 HOH   140 540 84  HOH   HOH BBB . 
J 5 HOH   141 541 278 HOH   HOH BBB . 
J 5 HOH   142 542 189 HOH   HOH BBB . 
J 5 HOH   143 543 137 HOH   HOH BBB . 
J 5 HOH   144 544 446 HOH   HOH BBB . 
J 5 HOH   145 545 226 HOH   HOH BBB . 
J 5 HOH   146 546 433 HOH   HOH BBB . 
J 5 HOH   147 547 185 HOH   HOH BBB . 
J 5 HOH   148 548 16  HOH   HOH BBB . 
J 5 HOH   149 549 41  HOH   HOH BBB . 
J 5 HOH   150 550 426 HOH   HOH BBB . 
J 5 HOH   151 551 268 HOH   HOH BBB . 
J 5 HOH   152 552 79  HOH   HOH BBB . 
J 5 HOH   153 553 133 HOH   HOH BBB . 
J 5 HOH   154 554 324 HOH   HOH BBB . 
J 5 HOH   155 555 68  HOH   HOH BBB . 
J 5 HOH   156 556 406 HOH   HOH BBB . 
J 5 HOH   157 557 34  HOH   HOH BBB . 
J 5 HOH   158 558 213 HOH   HOH BBB . 
J 5 HOH   159 559 142 HOH   HOH BBB . 
J 5 HOH   160 560 151 HOH   HOH BBB . 
J 5 HOH   161 561 410 HOH   HOH BBB . 
J 5 HOH   162 562 103 HOH   HOH BBB . 
J 5 HOH   163 563 90  HOH   HOH BBB . 
J 5 HOH   164 564 9   HOH   HOH BBB . 
J 5 HOH   165 565 366 HOH   HOH BBB . 
J 5 HOH   166 566 403 HOH   HOH BBB . 
J 5 HOH   167 567 53  HOH   HOH BBB . 
J 5 HOH   168 568 54  HOH   HOH BBB . 
J 5 HOH   169 569 59  HOH   HOH BBB . 
J 5 HOH   170 570 442 HOH   HOH BBB . 
J 5 HOH   171 571 312 HOH   HOH BBB . 
J 5 HOH   172 572 119 HOH   HOH BBB . 
J 5 HOH   173 573 373 HOH   HOH BBB . 
J 5 HOH   174 574 163 HOH   HOH BBB . 
J 5 HOH   175 575 368 HOH   HOH BBB . 
J 5 HOH   176 576 370 HOH   HOH BBB . 
J 5 HOH   177 577 405 HOH   HOH BBB . 
J 5 HOH   178 578 224 HOH   HOH BBB . 
J 5 HOH   179 579 274 HOH   HOH BBB . 
J 5 HOH   180 580 246 HOH   HOH BBB . 
J 5 HOH   181 581 387 HOH   HOH BBB . 
J 5 HOH   182 582 439 HOH   HOH BBB . 
J 5 HOH   183 583 296 HOH   HOH BBB . 
J 5 HOH   184 584 322 HOH   HOH BBB . 
J 5 HOH   185 585 347 HOH   HOH BBB . 
J 5 HOH   186 586 241 HOH   HOH BBB . 
J 5 HOH   187 587 318 HOH   HOH BBB . 
J 5 HOH   188 588 294 HOH   HOH BBB . 
J 5 HOH   189 589 441 HOH   HOH BBB . 
J 5 HOH   190 590 338 HOH   HOH BBB . 
J 5 HOH   191 591 337 HOH   HOH BBB . 
J 5 HOH   192 592 359 HOH   HOH BBB . 
J 5 HOH   193 593 430 HOH   HOH BBB . 
J 5 HOH   194 594 376 HOH   HOH BBB . 
J 5 HOH   195 595 388 HOH   HOH BBB . 
J 5 HOH   196 596 78  HOH   HOH BBB . 
J 5 HOH   197 597 367 HOH   HOH BBB . 
J 5 HOH   198 598 385 HOH   HOH BBB . 
J 5 HOH   199 599 140 HOH   HOH BBB . 
J 5 HOH   200 600 335 HOH   HOH BBB . 
J 5 HOH   201 601 343 HOH   HOH BBB . 
J 5 HOH   202 602 242 HOH   HOH BBB . 
J 5 HOH   203 603 386 HOH   HOH BBB . 
J 5 HOH   204 604 355 HOH   HOH BBB . 
J 5 HOH   205 605 339 HOH   HOH BBB . 
J 5 HOH   206 606 311 HOH   HOH BBB . 
J 5 HOH   207 607 300 HOH   HOH BBB . 
J 5 HOH   208 608 411 HOH   HOH BBB . 
J 5 HOH   209 609 323 HOH   HOH BBB . 
J 5 HOH   210 610 353 HOH   HOH BBB . 
J 5 HOH   211 611 282 HOH   HOH BBB . 
J 5 HOH   212 612 100 HOH   HOH BBB . 
J 5 HOH   213 613 329 HOH   HOH BBB . 
J 5 HOH   214 614 402 HOH   HOH BBB . 
J 5 HOH   215 615 351 HOH   HOH BBB . 
J 5 HOH   216 616 220 HOH   HOH BBB . 
J 5 HOH   217 617 223 HOH   HOH BBB . 
J 5 HOH   218 618 307 HOH   HOH BBB . 
J 5 HOH   219 619 416 HOH   HOH BBB . 
J 5 HOH   220 620 345 HOH   HOH BBB . 
J 5 HOH   221 621 348 HOH   HOH BBB . 
J 5 HOH   222 622 422 HOH   HOH BBB . 
J 5 HOH   223 623 331 HOH   HOH BBB . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 BBB ASP 9 ? CG  ? B ASP 10 CG  
2 1 Y 1 BBB ASP 9 ? OD1 ? B ASP 10 OD1 
3 1 Y 1 BBB ASP 9 ? OD2 ? B ASP 10 OD2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0258 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EP2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.640 
_cell.length_a_esd                 ? 
_cell.length_b                     70.900 
_cell.length_b_esd                 ? 
_cell.length_c                     121.250 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9EP2 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EP2 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.33 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.18 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              9.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '28-31% PEG4000, 0.2 M sodium acetate, 0.1 M Tris pH 9.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-04 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.00 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ELETTRA BEAMLINE 11.2C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11.2C 
_diffrn_source.pdbx_synchrotron_site       ELETTRA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EP2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.47 
_reflns.d_resolution_low                               61.20 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     92188 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.43 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17.35 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.078 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.074 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.47 
_reflns_shell.d_res_low                                     1.51 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.27 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6734 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               12.29 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               1.325 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.826 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.27 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -1.616 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            6.008 
_refine.aniso_B[2][3]                            -0.000 
_refine.aniso_B[3][3]                            -4.391 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               26.347 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.978 
_refine.correlation_coeff_Fo_to_Fc_free          0.967 
_refine.details                                  'Hydrogens have been added in their riding positions' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EP2 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.47 
_refine.ls_d_res_low                             61.20 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     92188 
_refine.ls_number_reflns_R_free                  4708 
_refine.ls_number_reflns_R_work                  87480 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.891 
_refine.ls_percent_reflns_R_free                 5.107 
_refine.ls_R_factor_all                          0.163 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2086 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1603 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'MASK BULK SOLVENT' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               NONE 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.076 
_refine.pdbx_overall_ESU_R_Free                  0.072 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             7.099 
_refine.overall_SU_ML                            0.103 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4042 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         56 
_refine_hist.number_atoms_solvent             442 
_refine_hist.number_atoms_total               4540 
_refine_hist.d_res_high                       1.47 
_refine_hist.d_res_low                        61.20 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.013  0.013  4284 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.017  3765 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.775  1.635  5846 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.500  1.586  8815 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 7.476  5.000  537  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 36.175 23.619 210  ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 12.772 15.000 679  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 19.446 15.000 15   ? r_dihedral_angle_4_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.093  0.200  544  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  4924 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  881  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.208  0.200  842  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.192  0.200  3615 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.167  0.200  2039 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.083  0.200  1784 ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.179  0.200  361  ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.080  0.200  3    ? r_symmetry_xyhbond_nbd_other   ? ? 
'X-RAY DIFFRACTION' ? 0.088  0.200  7    ? r_metal_ion_refined            ? ? 
'X-RAY DIFFRACTION' ? 0.212  0.200  19   ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.214  0.200  83   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.219  0.200  25   ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 3.582  2.534  2091 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 3.580  2.533  2090 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 3.903  3.818  2614 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 3.903  3.818  2615 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 5.117  2.905  2193 ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 5.116  2.905  2194 ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 5.671  4.205  3221 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 5.670  4.205  3222 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 5.566  31.305 4875 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 5.566  31.305 4876 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 12.796 3.000  8049 ? r_rigid_bond_restr             ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.471 1.509 . . 332 6382 99.6438  . . . . 0.302 . . . . . . . . . . . 0.332 
'X-RAY DIFFRACTION' 1.509 1.551 . . 324 6289 100.0000 . . . . 0.270 . . . . . . . . . . . 0.279 
'X-RAY DIFFRACTION' 1.551 1.596 . . 308 6064 99.9843  . . . . 0.245 . . . . . . . . . . . 0.289 
'X-RAY DIFFRACTION' 1.596 1.645 . . 340 5886 99.9198  . . . . 0.227 . . . . . . . . . . . 0.283 
'X-RAY DIFFRACTION' 1.645 1.699 . . 308 5705 100.0000 . . . . 0.210 . . . . . . . . . . . 0.256 
'X-RAY DIFFRACTION' 1.699 1.758 . . 310 5528 99.9658  . . . . 0.204 . . . . . . . . . . . 0.242 
'X-RAY DIFFRACTION' 1.758 1.825 . . 286 5346 99.9468  . . . . 0.180 . . . . . . . . . . . 0.224 
'X-RAY DIFFRACTION' 1.825 1.899 . . 299 5159 99.9268  . . . . 0.180 . . . . . . . . . . . 0.246 
'X-RAY DIFFRACTION' 1.899 1.983 . . 262 4910 99.8648  . . . . 0.162 . . . . . . . . . . . 0.225 
'X-RAY DIFFRACTION' 1.983 2.080 . . 255 4742 99.8801  . . . . 0.157 . . . . . . . . . . . 0.226 
'X-RAY DIFFRACTION' 2.080 2.192 . . 250 4507 99.9580  . . . . 0.150 . . . . . . . . . . . 0.214 
'X-RAY DIFFRACTION' 2.192 2.325 . . 194 4328 99.9116  . . . . 0.146 . . . . . . . . . . . 0.222 
'X-RAY DIFFRACTION' 2.325 2.485 . . 200 4053 99.9295  . . . . 0.140 . . . . . . . . . . . 0.202 
'X-RAY DIFFRACTION' 2.485 2.684 . . 212 3743 99.9242  . . . . 0.141 . . . . . . . . . . . 0.216 
'X-RAY DIFFRACTION' 2.684 2.940 . . 179 3494 99.9184  . . . . 0.134 . . . . . . . . . . . 0.184 
'X-RAY DIFFRACTION' 2.940 3.286 . . 167 3160 99.8499  . . . . 0.156 . . . . . . . . . . . 0.205 
'X-RAY DIFFRACTION' 3.286 3.792 . . 167 2801 99.9327  . . . . 0.159 . . . . . . . . . . . 0.219 
'X-RAY DIFFRACTION' 3.792 4.640 . . 131 2384 99.9603  . . . . 0.127 . . . . . . . . . . . 0.155 
'X-RAY DIFFRACTION' 4.640 6.544 . . 123 1877 100.0000 . . . . 0.137 . . . . . . . . . . . 0.174 
'X-RAY DIFFRACTION' 6.544 61.20 . . 61  1122 99.4118  . . . . 0.168 . . . . . . . . . . . 0.158 
# 
_struct.entry_id                     9EP2 
_struct.title                        
'Crystal structure of the complex of human carbonic anhydrase I with 4-sulfamoylphenyl 3-(p-tolylthio)propanoate' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9EP2 
_struct_keywords.text            'carbonic anhydrase, sulfonamide, inhibitor, metalloenzyme, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH1_HUMAN 
_struct_ref.pdbx_db_accession          P00915 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVL
KGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQK
VLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAV
PMQHNNRPTQPLKGRTVRASF
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9EP2 AAA 1 ? 261 ? P00915 1 ? 261 ? 0 260 
2 1 9EP2 BBB 1 ? 261 ? P00915 1 ? 261 ? 0 260 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,I 
2 1 B,G,H,J     
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 13  ? LEU A 20  ? GLY AAA 12  LEU AAA 19  5 ? 8  
HELX_P HELX_P2  AA2 TYR A 21  ? GLY A 26  ? TYR AAA 20  GLY AAA 25  5 ? 6  
HELX_P HELX_P3  AA3 ASN A 53  ? ALA A 55  ? ASN AAA 52  ALA AAA 54  5 ? 3  
HELX_P HELX_P4  AA4 SER A 131 ? ALA A 136 ? SER AAA 130 ALA AAA 135 1 ? 6  
HELX_P HELX_P5  AA5 ASN A 155 ? LYS A 157 ? ASN AAA 154 LYS AAA 156 5 ? 3  
HELX_P HELX_P6  AA6 LEU A 158 ? LEU A 165 ? LEU AAA 157 LEU AAA 164 1 ? 8  
HELX_P HELX_P7  AA7 GLN A 166 ? ILE A 168 ? GLN AAA 165 ILE AAA 167 5 ? 3  
HELX_P HELX_P8  AA8 ASP A 181 ? LEU A 186 ? ASP AAA 180 LEU AAA 185 5 ? 6  
HELX_P HELX_P9  AA9 SER A 220 ? SER A 229 ? SER AAA 219 SER AAA 228 1 ? 10 
HELX_P HELX_P10 AB1 GLY B 13  ? LEU B 20  ? GLY BBB 12  LEU BBB 19  5 ? 8  
HELX_P HELX_P11 AB2 TYR B 21  ? GLY B 26  ? TYR BBB 20  GLY BBB 25  5 ? 6  
HELX_P HELX_P12 AB3 LYS B 35  ? THR B 39  ? LYS BBB 34  THR BBB 38  5 ? 5  
HELX_P HELX_P13 AB4 ASN B 53  ? ALA B 55  ? ASN BBB 52  ALA BBB 54  5 ? 3  
HELX_P HELX_P14 AB5 SER B 131 ? ALA B 136 ? SER BBB 130 ALA BBB 135 1 ? 6  
HELX_P HELX_P15 AB6 ASN B 155 ? LYS B 157 ? ASN BBB 154 LYS BBB 156 5 ? 3  
HELX_P HELX_P16 AB7 LEU B 158 ? LEU B 165 ? LEU BBB 157 LEU BBB 164 1 ? 8  
HELX_P HELX_P17 AB8 GLN B 166 ? ILE B 168 ? GLN BBB 165 ILE BBB 167 5 ? 3  
HELX_P HELX_P18 AB9 ASP B 181 ? LEU B 186 ? ASP BBB 180 LEU BBB 185 5 ? 6  
HELX_P HELX_P19 AC1 SER B 220 ? SER B 229 ? SER BBB 219 SER BBB 228 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 95  NE2 ? ? ? 1_555 E ZN    . ZN  ? ? AAA HIS 94  AAA ZN    303 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc2 metalc ? ? A HIS 97  NE2 ? ? ? 1_555 E ZN    . ZN  ? ? AAA HIS 96  AAA ZN    303 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
metalc3 metalc ? ? A HIS 120 ND1 ? ? ? 1_555 E ZN    . ZN  ? ? AAA HIS 119 AAA ZN    303 1_555 ? ? ? ? ? ? ? 1.960 ? ? 
metalc4 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F A1H6C . N20 ? ? AAA ZN  303 AAA A1H6C 304 1_555 ? ? ? ? ? ? ? 1.923 ? ? 
metalc5 metalc ? ? B HIS 95  NE2 ? ? ? 1_555 G ZN    . ZN  ? ? BBB HIS 94  BBB ZN    301 1_555 ? ? ? ? ? ? ? 1.987 ? ? 
metalc6 metalc ? ? B HIS 97  NE2 ? ? ? 1_555 G ZN    . ZN  ? ? BBB HIS 96  BBB ZN    301 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
metalc7 metalc ? ? B HIS 120 ND1 ? ? ? 1_555 G ZN    . ZN  ? ? BBB HIS 119 BBB ZN    301 1_555 ? ? ? ? ? ? ? 1.955 ? ? 
metalc8 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 H A1H6C . N20 ? ? BBB ZN  301 BBB A1H6C 302 1_555 ? ? ? ? ? ? ? 1.967 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 95  ? AAA HIS 94  ? 1_555 ZN ? E ZN . ? AAA ZN 303 ? 1_555 NE2 ? A HIS   97  ? AAA HIS   96  ? 1_555 109.7 ? 
2  NE2 ? A HIS 95  ? AAA HIS 94  ? 1_555 ZN ? E ZN . ? AAA ZN 303 ? 1_555 ND1 ? A HIS   120 ? AAA HIS   119 ? 1_555 108.8 ? 
3  NE2 ? A HIS 97  ? AAA HIS 96  ? 1_555 ZN ? E ZN . ? AAA ZN 303 ? 1_555 ND1 ? A HIS   120 ? AAA HIS   119 ? 1_555 97.0  ? 
4  NE2 ? A HIS 95  ? AAA HIS 94  ? 1_555 ZN ? E ZN . ? AAA ZN 303 ? 1_555 N20 ? F A1H6C .   ? AAA A1H6C 304 ? 1_555 112.3 ? 
5  NE2 ? A HIS 97  ? AAA HIS 96  ? 1_555 ZN ? E ZN . ? AAA ZN 303 ? 1_555 N20 ? F A1H6C .   ? AAA A1H6C 304 ? 1_555 112.9 ? 
6  ND1 ? A HIS 120 ? AAA HIS 119 ? 1_555 ZN ? E ZN . ? AAA ZN 303 ? 1_555 N20 ? F A1H6C .   ? AAA A1H6C 304 ? 1_555 114.9 ? 
7  NE2 ? B HIS 95  ? BBB HIS 94  ? 1_555 ZN ? G ZN . ? BBB ZN 301 ? 1_555 NE2 ? B HIS   97  ? BBB HIS   96  ? 1_555 109.1 ? 
8  NE2 ? B HIS 95  ? BBB HIS 94  ? 1_555 ZN ? G ZN . ? BBB ZN 301 ? 1_555 ND1 ? B HIS   120 ? BBB HIS   119 ? 1_555 109.3 ? 
9  NE2 ? B HIS 97  ? BBB HIS 96  ? 1_555 ZN ? G ZN . ? BBB ZN 301 ? 1_555 ND1 ? B HIS   120 ? BBB HIS   119 ? 1_555 94.8  ? 
10 NE2 ? B HIS 95  ? BBB HIS 94  ? 1_555 ZN ? G ZN . ? BBB ZN 301 ? 1_555 N20 ? H A1H6C .   ? BBB A1H6C 302 ? 1_555 114.4 ? 
11 NE2 ? B HIS 97  ? BBB HIS 96  ? 1_555 ZN ? G ZN . ? BBB ZN 301 ? 1_555 N20 ? H A1H6C .   ? BBB A1H6C 302 ? 1_555 112.4 ? 
12 ND1 ? B HIS 120 ? BBB HIS 119 ? 1_555 ZN ? G ZN . ? BBB ZN 301 ? 1_555 N20 ? H A1H6C .   ? BBB A1H6C 302 ? 1_555 115.1 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 30  A . ? SER 29  AAA PRO 31  A ? PRO 30  AAA 1 1.61  
2 PRO 202 A . ? PRO 201 AAA PRO 203 A ? PRO 202 AAA 1 8.08  
3 SER 30  B . ? SER 29  BBB PRO 31  B ? PRO 30  BBB 1 -0.45 
4 PRO 202 B . ? PRO 201 BBB PRO 203 B ? PRO 202 BBB 1 9.72  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 33  ? ILE A 34  ? ASP AAA 32  ILE AAA 33  
AA1 2  THR A 109 ? VAL A 110 ? THR AAA 108 VAL AAA 109 
AA2 1  LYS A 40  ? HIS A 41  ? LYS AAA 39  HIS AAA 40  
AA2 2  ARG A 258 ? ALA A 259 ? ARG AAA 257 ALA AAA 258 
AA2 3  PHE A 192 ? GLY A 197 ? PHE AAA 191 GLY AAA 196 
AA2 4  VAL A 208 ? CYS A 213 ? VAL AAA 207 CYS AAA 212 
AA2 5  LEU A 142 ? VAL A 151 ? LEU AAA 141 VAL AAA 150 
AA2 6  ALA A 117 ? ASN A 125 ? ALA AAA 116 ASN AAA 124 
AA2 7  TYR A 89  ? TRP A 98  ? TYR AAA 88  TRP AAA 97  
AA2 8  PHE A 67  ? PHE A 71  ? PHE AAA 66  PHE AAA 70  
AA2 9  ALA A 57  ? ASN A 62  ? ALA AAA 56  ASN AAA 61  
AA2 10 ARG A 174 ? PRO A 176 ? ARG AAA 173 PRO AAA 175 
AA3 1  ILE A 48  ? SER A 51  ? ILE AAA 47  SER AAA 50  
AA3 2  VAL A 79  ? GLY A 82  ? VAL AAA 78  GLY AAA 81  
AA3 3  TYR A 89  ? TRP A 98  ? TYR AAA 88  TRP AAA 97  
AA3 4  ALA A 117 ? ASN A 125 ? ALA AAA 116 ASN AAA 124 
AA3 5  LEU A 142 ? VAL A 151 ? LEU AAA 141 VAL AAA 150 
AA3 6  ILE A 217 ? VAL A 219 ? ILE AAA 216 VAL AAA 218 
AA4 1  ASP B 33  ? ILE B 34  ? ASP BBB 32  ILE BBB 33  
AA4 2  THR B 109 ? VAL B 110 ? THR BBB 108 VAL BBB 109 
AA5 1  LYS B 40  ? HIS B 41  ? LYS BBB 39  HIS BBB 40  
AA5 2  ARG B 258 ? ALA B 259 ? ARG BBB 257 ALA BBB 258 
AA5 3  PHE B 192 ? GLY B 197 ? PHE BBB 191 GLY BBB 196 
AA5 4  VAL B 208 ? CYS B 213 ? VAL BBB 207 CYS BBB 212 
AA5 5  LEU B 142 ? VAL B 151 ? LEU BBB 141 VAL BBB 150 
AA5 6  ALA B 117 ? TRP B 124 ? ALA BBB 116 TRP BBB 123 
AA5 7  TYR B 89  ? TRP B 98  ? TYR BBB 88  TRP BBB 97  
AA5 8  PHE B 67  ? PHE B 71  ? PHE BBB 66  PHE BBB 70  
AA5 9  ALA B 57  ? ASN B 62  ? ALA BBB 56  ASN BBB 61  
AA5 10 ARG B 174 ? PRO B 176 ? ARG BBB 173 PRO BBB 175 
AA6 1  ILE B 48  ? SER B 51  ? ILE BBB 47  SER BBB 50  
AA6 2  VAL B 79  ? GLY B 82  ? VAL BBB 78  GLY BBB 81  
AA6 3  TYR B 89  ? TRP B 98  ? TYR BBB 88  TRP BBB 97  
AA6 4  ALA B 117 ? TRP B 124 ? ALA BBB 116 TRP BBB 123 
AA6 5  LEU B 142 ? VAL B 151 ? LEU BBB 141 VAL BBB 150 
AA6 6  ILE B 217 ? VAL B 219 ? ILE BBB 216 VAL BBB 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 34  ? N ILE AAA 33  O THR A 109 ? O THR AAA 108 
AA2 1 2  N LYS A 40  ? N LYS AAA 39  O ALA A 259 ? O ALA AAA 258 
AA2 2 3  O ARG A 258 ? O ARG AAA 257 N THR A 194 ? N THR AAA 193 
AA2 3 4  N GLY A 197 ? N GLY AAA 196 O VAL A 208 ? O VAL AAA 207 
AA2 4 5  O ILE A 211 ? O ILE AAA 210 N GLY A 146 ? N GLY AAA 145 
AA2 5 6  O MET A 149 ? O MET AAA 148 N ALA A 117 ? N ALA AAA 116 
AA2 6 7  O TRP A 124 ? O TRP AAA 123 N ARG A 90  ? N ARG AAA 89  
AA2 7 8  O PHE A 94  ? O PHE AAA 93  N VAL A 69  ? N VAL AAA 68  
AA2 8 9  O ASN A 70  ? O ASN AAA 69  N LYS A 58  ? N LYS AAA 57  
AA2 9 10 N ILE A 60  ? N ILE AAA 59  O ALA A 175 ? O ALA AAA 174 
AA3 1 2  N SER A 49  ? N SER AAA 48  O LYS A 81  ? O LYS AAA 80  
AA3 2 3  N LEU A 80  ? N LEU AAA 79  O TYR A 89  ? O TYR AAA 88  
AA3 3 4  N ARG A 90  ? N ARG AAA 89  O TRP A 124 ? O TRP AAA 123 
AA3 4 5  N ALA A 117 ? N ALA AAA 116 O MET A 149 ? O MET AAA 148 
AA3 5 6  N LYS A 150 ? N LYS AAA 149 O ILE A 217 ? O ILE AAA 216 
AA4 1 2  N ILE B 34  ? N ILE BBB 33  O THR B 109 ? O THR BBB 108 
AA5 1 2  N LYS B 40  ? N LYS BBB 39  O ALA B 259 ? O ALA BBB 258 
AA5 2 3  O ARG B 258 ? O ARG BBB 257 N THR B 194 ? N THR BBB 193 
AA5 3 4  N GLY B 197 ? N GLY BBB 196 O VAL B 208 ? O VAL BBB 207 
AA5 4 5  O ILE B 211 ? O ILE BBB 210 N GLY B 146 ? N GLY BBB 145 
AA5 5 6  O VAL B 147 ? O VAL BBB 146 N LEU B 119 ? N LEU BBB 118 
AA5 6 7  O HIS B 120 ? O HIS BBB 119 N HIS B 95  ? N HIS BBB 94  
AA5 7 8  O PHE B 92  ? O PHE BBB 91  N PHE B 71  ? N PHE BBB 70  
AA5 8 9  O ASN B 70  ? O ASN BBB 69  N GLU B 59  ? N GLU BBB 58  
AA5 9 10 N ILE B 60  ? N ILE BBB 59  O ALA B 175 ? O ALA BBB 174 
AA6 1 2  N SER B 49  ? N SER BBB 48  O LYS B 81  ? O LYS BBB 80  
AA6 2 3  N LEU B 80  ? N LEU BBB 79  O TYR B 89  ? O TYR BBB 88  
AA6 3 4  N HIS B 95  ? N HIS BBB 94  O HIS B 120 ? O HIS BBB 119 
AA6 4 5  N LEU B 119 ? N LEU BBB 118 O VAL B 147 ? O VAL BBB 146 
AA6 5 6  N LYS B 150 ? N LYS BBB 149 O ILE B 217 ? O ILE BBB 216 
# 
_pdbx_entry_details.entry_id                   9EP2 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CD AAA GLU 14  ? ? OE2 AAA GLU 14  ? ? 1.324 1.252 0.072 0.011 N 
2 1 C  BBB SER 50  ? ? O   BBB SER 50  ? ? 1.357 1.229 0.128 0.019 N 
3 1 CD BBB GLU 106 ? ? OE2 BBB GLU 106 ? ? 1.331 1.252 0.079 0.011 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN AAA 75  ? ? -95.24  34.76  
2  1 GLU AAA 106 ? ? -92.83  -61.07 
3  1 ASN AAA 244 ? ? -159.12 31.28  
4  1 LYS BBB 10  ? ? 157.69  -51.92 
5  1 LYS BBB 57  ? ? -124.78 -60.97 
6  1 ASN BBB 75  ? ? -99.96  44.25  
7  1 HIS BBB 103 ? ? -168.28 106.89 
8  1 GLU BBB 106 ? ? -101.56 -62.45 
9  1 ASN BBB 178 ? ? 61.40   60.95  
10 1 ASN BBB 244 ? ? -162.03 34.73  
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 SER BBB 50 ? A 10.57 
2 1 SER BBB 50 ? B 14.85 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      AAA 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       619 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.16 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 AAA MET 0 ? A MET 1 
2 1 Y 1 AAA ALA 1 ? A ALA 2 
3 1 Y 1 AAA SER 2 ? A SER 3 
4 1 Y 1 AAA PRO 3 ? A PRO 4 
5 1 Y 1 BBB MET 0 ? B MET 1 
6 1 Y 1 BBB ALA 1 ? B ALA 2 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1H6C C2   C  N N 1   
A1H6C C3   C  N N 2   
A1H6C C4   C  N N 3   
A1H6C C6   C  Y N 4   
A1H6C C7   C  Y N 5   
A1H6C C8   C  Y N 6   
A1H6C C9   C  Y N 7   
A1H6C C10  C  N N 8   
A1H6C C11  C  Y N 9   
A1H6C C12  C  Y N 10  
A1H6C C14  C  Y N 11  
A1H6C C15  C  Y N 12  
A1H6C C16  C  Y N 13  
A1H6C C17  C  Y N 14  
A1H6C O1   O  N N 15  
A1H6C S5   S  N N 16  
A1H6C O13  O  N N 17  
A1H6C S18  S  N N 18  
A1H6C O19  O  N N 19  
A1H6C N20  N  N N 20  
A1H6C O21  O  N N 21  
A1H6C C22  C  Y N 22  
A1H6C C23  C  Y N 23  
A1H6C H3B  H  N N 24  
A1H6C H3A  H  N N 25  
A1H6C H4A  H  N N 26  
A1H6C H4B  H  N N 27  
A1H6C H7   H  N N 28  
A1H6C H8   H  N N 29  
A1H6C H10C H  N N 30  
A1H6C H10B H  N N 31  
A1H6C H10A H  N N 32  
A1H6C H11  H  N N 33  
A1H6C H12  H  N N 34  
A1H6C H15  H  N N 35  
A1H6C H16  H  N N 36  
A1H6C H20B H  N N 37  
A1H6C H20A H  N N 38  
A1H6C H22  H  N N 39  
A1H6C H23  H  N N 40  
ACT   C    C  N N 41  
ACT   O    O  N N 42  
ACT   OXT  O  N N 43  
ACT   CH3  C  N N 44  
ACT   H1   H  N N 45  
ACT   H2   H  N N 46  
ACT   H3   H  N N 47  
ALA   N    N  N N 48  
ALA   CA   C  N S 49  
ALA   C    C  N N 50  
ALA   O    O  N N 51  
ALA   CB   C  N N 52  
ALA   OXT  O  N N 53  
ALA   H    H  N N 54  
ALA   H2   H  N N 55  
ALA   HA   H  N N 56  
ALA   HB1  H  N N 57  
ALA   HB2  H  N N 58  
ALA   HB3  H  N N 59  
ALA   HXT  H  N N 60  
ARG   N    N  N N 61  
ARG   CA   C  N S 62  
ARG   C    C  N N 63  
ARG   O    O  N N 64  
ARG   CB   C  N N 65  
ARG   CG   C  N N 66  
ARG   CD   C  N N 67  
ARG   NE   N  N N 68  
ARG   CZ   C  N N 69  
ARG   NH1  N  N N 70  
ARG   NH2  N  N N 71  
ARG   OXT  O  N N 72  
ARG   H    H  N N 73  
ARG   H2   H  N N 74  
ARG   HA   H  N N 75  
ARG   HB2  H  N N 76  
ARG   HB3  H  N N 77  
ARG   HG2  H  N N 78  
ARG   HG3  H  N N 79  
ARG   HD2  H  N N 80  
ARG   HD3  H  N N 81  
ARG   HE   H  N N 82  
ARG   HH11 H  N N 83  
ARG   HH12 H  N N 84  
ARG   HH21 H  N N 85  
ARG   HH22 H  N N 86  
ARG   HXT  H  N N 87  
ASN   N    N  N N 88  
ASN   CA   C  N S 89  
ASN   C    C  N N 90  
ASN   O    O  N N 91  
ASN   CB   C  N N 92  
ASN   CG   C  N N 93  
ASN   OD1  O  N N 94  
ASN   ND2  N  N N 95  
ASN   OXT  O  N N 96  
ASN   H    H  N N 97  
ASN   H2   H  N N 98  
ASN   HA   H  N N 99  
ASN   HB2  H  N N 100 
ASN   HB3  H  N N 101 
ASN   HD21 H  N N 102 
ASN   HD22 H  N N 103 
ASN   HXT  H  N N 104 
ASP   N    N  N N 105 
ASP   CA   C  N S 106 
ASP   C    C  N N 107 
ASP   O    O  N N 108 
ASP   CB   C  N N 109 
ASP   CG   C  N N 110 
ASP   OD1  O  N N 111 
ASP   OD2  O  N N 112 
ASP   OXT  O  N N 113 
ASP   H    H  N N 114 
ASP   H2   H  N N 115 
ASP   HA   H  N N 116 
ASP   HB2  H  N N 117 
ASP   HB3  H  N N 118 
ASP   HD2  H  N N 119 
ASP   HXT  H  N N 120 
CYS   N    N  N N 121 
CYS   CA   C  N R 122 
CYS   C    C  N N 123 
CYS   O    O  N N 124 
CYS   CB   C  N N 125 
CYS   SG   S  N N 126 
CYS   OXT  O  N N 127 
CYS   H    H  N N 128 
CYS   H2   H  N N 129 
CYS   HA   H  N N 130 
CYS   HB2  H  N N 131 
CYS   HB3  H  N N 132 
CYS   HG   H  N N 133 
CYS   HXT  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
ZN    ZN   ZN N N 438 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1H6C O1  C2   doub N N 1   
A1H6C C2  C3   sing N N 2   
A1H6C C3  C4   sing N N 3   
A1H6C C4  S5   sing N N 4   
A1H6C S5  C6   sing N N 5   
A1H6C C6  C7   doub Y N 6   
A1H6C C7  C8   sing Y N 7   
A1H6C C8  C9   doub Y N 8   
A1H6C C9  C10  sing N N 9   
A1H6C C9  C11  sing Y N 10  
A1H6C C11 C12  doub Y N 11  
A1H6C C2  O13  sing N N 12  
A1H6C O13 C14  sing N N 13  
A1H6C C14 C15  doub Y N 14  
A1H6C C15 C16  sing Y N 15  
A1H6C C16 C17  doub Y N 16  
A1H6C C17 S18  sing N N 17  
A1H6C S18 O19  doub N N 18  
A1H6C S18 N20  sing N N 19  
A1H6C S18 O21  doub N N 20  
A1H6C C17 C22  sing Y N 21  
A1H6C C22 C23  doub Y N 22  
A1H6C C12 C6   sing Y N 23  
A1H6C C23 C14  sing Y N 24  
A1H6C C3  H3B  sing N N 25  
A1H6C C3  H3A  sing N N 26  
A1H6C C4  H4A  sing N N 27  
A1H6C C4  H4B  sing N N 28  
A1H6C C7  H7   sing N N 29  
A1H6C C8  H8   sing N N 30  
A1H6C C10 H10C sing N N 31  
A1H6C C10 H10B sing N N 32  
A1H6C C10 H10A sing N N 33  
A1H6C C11 H11  sing N N 34  
A1H6C C12 H12  sing N N 35  
A1H6C C15 H15  sing N N 36  
A1H6C C16 H16  sing N N 37  
A1H6C N20 H20B sing N N 38  
A1H6C N20 H20A sing N N 39  
A1H6C C22 H22  sing N N 40  
A1H6C C23 H23  sing N N 41  
ACT   C   O    doub N N 42  
ACT   C   OXT  sing N N 43  
ACT   C   CH3  sing N N 44  
ACT   CH3 H1   sing N N 45  
ACT   CH3 H2   sing N N 46  
ACT   CH3 H3   sing N N 47  
ALA   N   CA   sing N N 48  
ALA   N   H    sing N N 49  
ALA   N   H2   sing N N 50  
ALA   CA  C    sing N N 51  
ALA   CA  CB   sing N N 52  
ALA   CA  HA   sing N N 53  
ALA   C   O    doub N N 54  
ALA   C   OXT  sing N N 55  
ALA   CB  HB1  sing N N 56  
ALA   CB  HB2  sing N N 57  
ALA   CB  HB3  sing N N 58  
ALA   OXT HXT  sing N N 59  
ARG   N   CA   sing N N 60  
ARG   N   H    sing N N 61  
ARG   N   H2   sing N N 62  
ARG   CA  C    sing N N 63  
ARG   CA  CB   sing N N 64  
ARG   CA  HA   sing N N 65  
ARG   C   O    doub N N 66  
ARG   C   OXT  sing N N 67  
ARG   CB  CG   sing N N 68  
ARG   CB  HB2  sing N N 69  
ARG   CB  HB3  sing N N 70  
ARG   CG  CD   sing N N 71  
ARG   CG  HG2  sing N N 72  
ARG   CG  HG3  sing N N 73  
ARG   CD  NE   sing N N 74  
ARG   CD  HD2  sing N N 75  
ARG   CD  HD3  sing N N 76  
ARG   NE  CZ   sing N N 77  
ARG   NE  HE   sing N N 78  
ARG   CZ  NH1  sing N N 79  
ARG   CZ  NH2  doub N N 80  
ARG   NH1 HH11 sing N N 81  
ARG   NH1 HH12 sing N N 82  
ARG   NH2 HH21 sing N N 83  
ARG   NH2 HH22 sing N N 84  
ARG   OXT HXT  sing N N 85  
ASN   N   CA   sing N N 86  
ASN   N   H    sing N N 87  
ASN   N   H2   sing N N 88  
ASN   CA  C    sing N N 89  
ASN   CA  CB   sing N N 90  
ASN   CA  HA   sing N N 91  
ASN   C   O    doub N N 92  
ASN   C   OXT  sing N N 93  
ASN   CB  CG   sing N N 94  
ASN   CB  HB2  sing N N 95  
ASN   CB  HB3  sing N N 96  
ASN   CG  OD1  doub N N 97  
ASN   CG  ND2  sing N N 98  
ASN   ND2 HD21 sing N N 99  
ASN   ND2 HD22 sing N N 100 
ASN   OXT HXT  sing N N 101 
ASP   N   CA   sing N N 102 
ASP   N   H    sing N N 103 
ASP   N   H2   sing N N 104 
ASP   CA  C    sing N N 105 
ASP   CA  CB   sing N N 106 
ASP   CA  HA   sing N N 107 
ASP   C   O    doub N N 108 
ASP   C   OXT  sing N N 109 
ASP   CB  CG   sing N N 110 
ASP   CB  HB2  sing N N 111 
ASP   CB  HB3  sing N N 112 
ASP   CG  OD1  doub N N 113 
ASP   CG  OD2  sing N N 114 
ASP   OD2 HD2  sing N N 115 
ASP   OXT HXT  sing N N 116 
CYS   N   CA   sing N N 117 
CYS   N   H    sing N N 118 
CYS   N   H2   sing N N 119 
CYS   CA  C    sing N N 120 
CYS   CA  CB   sing N N 121 
CYS   CA  HA   sing N N 122 
CYS   C   O    doub N N 123 
CYS   C   OXT  sing N N 124 
CYS   CB  SG   sing N N 125 
CYS   CB  HB2  sing N N 126 
CYS   CB  HB3  sing N N 127 
CYS   SG  HG   sing N N 128 
CYS   OXT HXT  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1JV0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EP2 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.015964 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014104 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.008247 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C  6  6  2.310  20.844 1.020 10.208 1.589 0.569  0.865 51.651 0.216   
H  1  1  0.493  10.511 0.323 26.126 0.140 3.142  0.041 57.800 0.003   
N  7  7  12.222 0.006  3.135 9.893  2.014 28.997 1.167 0.583  -11.538 
O  8  8  3.049  13.277 2.287 5.701  1.546 0.324  0.867 32.909 0.251   
S  16 16 6.905  1.468  5.203 22.215 1.438 0.254  1.586 56.172 1.056   
ZN 30 30 14.082 3.266  7.036 0.233  5.165 10.316 2.411 58.710 0.909   
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
_atom_site.calc_flag 
ATOM   1    N  N   . ASP   A 1 5   ? -14.553 27.844 55.101 1.000 71.806  ? 4   ASP   AAA N   1 ? 
ATOM   2    C  CA  . ASP   A 1 5   ? -14.810 26.373 55.202 1.000 56.358  ? 4   ASP   AAA CA  1 ? 
ATOM   3    C  C   . ASP   A 1 5   ? -14.426 25.666 53.889 1.000 47.708  ? 4   ASP   AAA C   1 ? 
ATOM   4    O  O   . ASP   A 1 5   ? -13.585 24.717 53.932 1.000 61.548  ? 4   ASP   AAA O   1 ? 
ATOM   5    C  CB  . ASP   A 1 5   ? -16.275 26.095 55.533 1.000 59.175  ? 4   ASP   AAA CB  1 ? 
ATOM   6    C  CG  . ASP   A 1 5   ? -16.483 24.693 56.071 1.000 63.564  ? 4   ASP   AAA CG  1 ? 
ATOM   7    O  OD1 . ASP   A 1 5   ? -15.540 24.193 56.741 1.000 73.907  ? 4   ASP   AAA OD1 1 ? 
ATOM   8    O  OD2 . ASP   A 1 5   ? -17.589 24.116 55.838 1.000 90.535  ? 4   ASP   AAA OD2 1 ? 
ATOM   9    N  N   . TRP   A 1 6   ? -15.037 26.076 52.767 1.000 36.477  ? 5   TRP   AAA N   1 ? 
ATOM   10   C  CA  . TRP   A 1 6   ? -14.597 25.704 51.400 1.000 31.710  ? 5   TRP   AAA CA  1 ? 
ATOM   11   C  C   . TRP   A 1 6   ? -13.310 26.470 51.104 1.000 28.730  ? 5   TRP   AAA C   1 ? 
ATOM   12   O  O   . TRP   A 1 6   ? -13.106 27.514 51.712 1.000 28.773  ? 5   TRP   AAA O   1 ? 
ATOM   13   C  CB  . TRP   A 1 6   ? -15.675 25.978 50.347 1.000 29.836  ? 5   TRP   AAA CB  1 ? 
ATOM   14   C  CG  . TRP   A 1 6   ? -15.955 27.416 50.090 1.000 28.021  ? 5   TRP   AAA CG  1 ? 
ATOM   15   C  CD1 . TRP   A 1 6   ? -16.956 28.162 50.624 1.000 28.393  ? 5   TRP   AAA CD1 1 ? 
ATOM   16   C  CD2 . TRP   A 1 6   ? -15.230 28.254 49.182 1.000 23.158  ? 5   TRP   AAA CD2 1 ? 
ATOM   17   N  NE1 . TRP   A 1 6   ? -16.883 29.447 50.136 1.000 25.650  ? 5   TRP   AAA NE1 1 ? 
ATOM   18   C  CE2 . TRP   A 1 6   ? -15.855 29.517 49.225 1.000 22.853  ? 5   TRP   AAA CE2 1 ? 
ATOM   19   C  CE3 . TRP   A 1 6   ? -14.113 28.058 48.360 1.000 25.843  ? 5   TRP   AAA CE3 1 ? 
ATOM   20   C  CZ2 . TRP   A 1 6   ? -15.340 30.581 48.490 1.000 25.621  ? 5   TRP   AAA CZ2 1 ? 
ATOM   21   C  CZ3 . TRP   A 1 6   ? -13.661 29.092 47.574 1.000 22.179  ? 5   TRP   AAA CZ3 1 ? 
ATOM   22   C  CH2 . TRP   A 1 6   ? -14.262 30.352 47.670 1.000 23.151  ? 5   TRP   AAA CH2 1 ? 
ATOM   23   N  N   . GLY   A 1 7   ? -12.488 25.931 50.215 1.000 29.262  ? 6   GLY   AAA N   1 ? 
ATOM   24   C  CA  . GLY   A 1 7   ? -11.184 26.484 49.832 1.000 28.254  ? 6   GLY   AAA CA  1 ? 
ATOM   25   C  C   . GLY   A 1 7   ? -10.699 25.839 48.532 1.000 27.651  ? 6   GLY   AAA C   1 ? 
ATOM   26   O  O   . GLY   A 1 7   ? -11.524 25.501 47.677 1.000 28.469  ? 6   GLY   AAA O   1 ? 
ATOM   27   N  N   . TYR   A 1 8   ? -9.379  25.769 48.411 1.000 29.384  ? 7   TYR   AAA N   1 ? 
ATOM   28   C  CA  . TYR   A 1 8   ? -8.673  25.241 47.222 1.000 29.003  ? 7   TYR   AAA CA  1 ? 
ATOM   29   C  C   . TYR   A 1 8   ? -7.686  24.145 47.668 1.000 36.497  ? 7   TYR   AAA C   1 ? 
ATOM   30   O  O   . TYR   A 1 8   ? -6.999  23.660 46.777 1.000 42.326  ? 7   TYR   AAA O   1 ? 
ATOM   31   C  CB  . TYR   A 1 8   ? -8.002  26.359 46.418 1.000 25.765  ? 7   TYR   AAA CB  1 ? 
ATOM   32   C  CG  . TYR   A 1 8   ? -9.019  27.287 45.787 1.000 25.230  ? 7   TYR   AAA CG  1 ? 
ATOM   33   C  CD1 . TYR   A 1 8   ? -9.546  27.033 44.528 1.000 26.420  ? 7   TYR   AAA CD1 1 ? 
ATOM   34   C  CD2 . TYR   A 1 8   ? -9.377  28.485 46.390 1.000 21.728  ? 7   TYR   AAA CD2 1 ? 
ATOM   35   C  CE1 . TYR   A 1 8   ? -10.513 27.829 43.932 1.000 21.964  ? 7   TYR   AAA CE1 1 ? 
ATOM   36   C  CE2 . TYR   A 1 8   ? -10.352 29.272 45.815 1.000 20.658  ? 7   TYR   AAA CE2 1 ? 
ATOM   37   C  CZ  . TYR   A 1 8   ? -10.899 28.993 44.573 1.000 20.331  ? 7   TYR   AAA CZ  1 ? 
ATOM   38   O  OH  . TYR   A 1 8   ? -11.785 29.892 44.004 1.000 19.898  ? 7   TYR   AAA OH  1 ? 
ATOM   39   N  N   . ASP   A 1 9   ? -7.575  23.847 48.978 1.000 30.957  ? 8   ASP   AAA N   1 ? 
ATOM   40   C  CA  . ASP   A 1 9   ? -6.645  22.763 49.435 1.000 36.075  ? 8   ASP   AAA CA  1 ? 
ATOM   41   C  C   . ASP   A 1 9   ? -7.310  21.409 49.131 1.000 41.057  ? 8   ASP   AAA C   1 ? 
ATOM   42   O  O   . ASP   A 1 9   ? -8.473  21.400 48.685 1.000 37.340  ? 8   ASP   AAA O   1 ? 
ATOM   43   C  CB  . ASP   A 1 9   ? -6.155  22.954 50.883 1.000 44.726  ? 8   ASP   AAA CB  1 ? 
ATOM   44   C  CG  . ASP   A 1 9   ? -7.143  22.655 52.004 1.000 62.533  ? 8   ASP   AAA CG  1 ? 
ATOM   45   O  OD1 . ASP   A 1 9   ? -7.986  21.726 51.831 1.000 69.349  ? 8   ASP   AAA OD1 1 ? 
ATOM   46   O  OD2 . ASP   A 1 9   ? -7.044  23.344 53.069 1.000 77.920  ? 8   ASP   AAA OD2 1 ? 
ATOM   47   N  N   . ASP   A 1 10  ? -6.573  20.309 49.306 1.000 49.772  ? 9   ASP   AAA N   1 ? 
ATOM   48   C  CA  . ASP   A 1 10  ? -7.070  18.953 48.935 1.000 53.041  ? 9   ASP   AAA CA  1 ? 
ATOM   49   C  C   . ASP   A 1 10  ? -8.397  18.651 49.656 1.000 45.262  ? 9   ASP   AAA C   1 ? 
ATOM   50   O  O   . ASP   A 1 10  ? -9.339  18.175 48.989 1.000 60.620  ? 9   ASP   AAA O   1 ? 
ATOM   51   C  CB  . ASP   A 1 10  ? -6.027  17.877 49.254 1.000 62.604  ? 9   ASP   AAA CB  1 ? 
ATOM   52   C  CG  . ASP   A 1 10  ? -4.669  18.198 48.653 1.000 69.347  ? 9   ASP   AAA CG  1 ? 
ATOM   53   O  OD1 . ASP   A 1 10  ? -4.631  19.038 47.706 1.000 72.960  ? 9   ASP   AAA OD1 1 ? 
ATOM   54   O  OD2 . ASP   A 1 10  ? -3.659  17.643 49.156 1.000 67.287  ? 9   ASP   AAA OD2 1 ? 
ATOM   55   N  N   . LYS   A 1 11  ? -8.473  18.927 50.963 1.000 44.482  ? 10  LYS   AAA N   1 ? 
ATOM   56   C  CA  . LYS   A 1 11  ? -9.665  18.545 51.799 1.000 44.869  ? 10  LYS   AAA CA  1 ? 
ATOM   57   C  C   . LYS   A 1 11  ? -10.914 19.401 51.475 1.000 43.016  ? 10  LYS   AAA C   1 ? 
ATOM   58   O  O   . LYS   A 1 11  ? -12.043 18.838 51.517 1.000 56.315  ? 10  LYS   AAA O   1 ? 
ATOM   59   C  CB  . LYS   A 1 11  ? -9.343  18.650 53.292 1.000 56.932  ? 10  LYS   AAA CB  1 ? 
ATOM   60   C  CG  . LYS   A 1 11  ? -10.281 17.840 54.179 1.000 57.326  ? 10  LYS   AAA CG  1 ? 
ATOM   61   C  CD  . LYS   A 1 11  ? -9.647  16.630 54.825 1.000 50.531  ? 10  LYS   AAA CD  1 ? 
ATOM   62   C  CE  . LYS   A 1 11  ? -10.219 16.381 56.202 1.000 53.018  ? 10  LYS   AAA CE  1 ? 
ATOM   63   N  NZ  . LYS   A 1 11  ? -9.080  16.082 57.204 1.000 36.347  ? 10  LYS   AAA NZ  1 ? 
ATOM   64   N  N   . ASN   A 1 12  ? -10.763 20.705 51.191 1.000 41.285  ? 11  ASN   AAA N   1 ? 
ATOM   65   C  CA  . ASN   A 1 12  ? -11.939 21.625 51.079 1.000 36.765  ? 11  ASN   AAA CA  1 ? 
ATOM   66   C  C   . ASN   A 1 12  ? -12.072 22.191 49.656 1.000 31.771  ? 11  ASN   AAA C   1 ? 
ATOM   67   O  O   . ASN   A 1 12  ? -12.886 23.147 49.457 1.000 30.278  ? 11  ASN   AAA O   1 ? 
ATOM   68   C  CB  . ASN   A 1 12  ? -11.865 22.736 52.132 1.000 37.565  ? 11  ASN   AAA CB  1 ? 
ATOM   69   C  CG  . ASN   A 1 12  ? -10.676 23.676 51.968 1.000 40.219  ? 11  ASN   AAA CG  1 ? 
ATOM   70   O  OD1 . ASN   A 1 12  ? -9.956  23.635 50.960 1.000 33.214  ? 11  ASN   AAA OD1 1 ? 
ATOM   71   N  ND2 . ASN   A 1 12  ? -10.457 24.536 52.954 1.000 34.022  ? 11  ASN   AAA ND2 1 ? 
ATOM   72   N  N   . GLY   A 1 13  ? -11.320 21.643 48.696 1.000 32.410  ? 12  GLY   AAA N   1 ? 
ATOM   73   C  CA  . GLY   A 1 13  ? -11.136 22.179 47.337 1.000 27.551  ? 12  GLY   AAA CA  1 ? 
ATOM   74   C  C   . GLY   A 1 13  ? -12.266 21.821 46.356 1.000 23.771  ? 12  GLY   AAA C   1 ? 
ATOM   75   O  O   . GLY   A 1 13  ? -13.314 21.267 46.703 1.000 34.991  ? 12  GLY   AAA O   1 ? 
ATOM   76   N  N   . PRO   A 1 14  ? -12.043 22.269 45.064 1.000 26.370  ? 13  PRO   AAA N   1 ? 
ATOM   77   C  CA  . PRO   A 1 14  ? -13.014 22.035 44.002 1.000 30.597  ? 13  PRO   AAA CA  1 ? 
ATOM   78   C  C   . PRO   A 1 14  ? -13.616 20.626 43.957 1.000 32.679  ? 13  PRO   AAA C   1 ? 
ATOM   79   O  O   . PRO   A 1 14  ? -14.802 20.542 43.697 1.000 31.400  ? 13  PRO   AAA O   1 ? 
ATOM   80   C  CB  . PRO   A 1 14  ? -12.194 22.268 42.731 1.000 34.577  ? 13  PRO   AAA CB  1 ? 
ATOM   81   C  CG  . PRO   A 1 14  ? -11.218 23.383 43.121 1.000 30.252  ? 13  PRO   AAA CG  1 ? 
ATOM   82   C  CD  . PRO   A 1 14  ? -10.899 23.108 44.582 1.000 33.051  ? 13  PRO   AAA CD  1 ? 
ATOM   83   N  N   . GLU   A 1 15  ? -12.809 19.573 44.150 1.000 38.723  ? 14  GLU   AAA N   1 ? 
ATOM   84   C  CA  . GLU   A 1 15  ? -13.315 18.179 44.008 1.000 40.723  ? 14  GLU   AAA CA  1 ? 
ATOM   85   C  C   . GLU   A 1 15  ? -14.362 17.858 45.094 1.000 39.597  ? 14  GLU   AAA C   1 ? 
ATOM   86   O  O   . GLU   A 1 15  ? -15.196 16.945 44.856 1.000 51.490  ? 14  GLU   AAA O   1 ? 
ATOM   87   C  CB  . GLU   A 1 15  ? -12.115 17.229 43.976 1.000 55.572  ? 14  GLU   AAA CB  1 ? 
ATOM   88   C  CG  . GLU   A 1 15  ? -11.279 17.373 42.705 1.000 58.328  ? 14  GLU   AAA CG  1 ? 
ATOM   89   C  CD  . GLU   A 1 15  ? -12.069 17.533 41.380 1.000 82.711  ? 14  GLU   AAA CD  1 ? 
ATOM   90   O  OE1 . GLU   A 1 15  ? -11.635 18.471 40.577 1.000 74.479  ? 14  GLU   AAA OE1 1 ? 
ATOM   91   O  OE2 . GLU   A 1 15  ? -13.083 16.722 41.123 1.000 71.219  ? 14  GLU   AAA OE2 1 ? 
ATOM   92   N  N   . GLN   A 1 16  ? -14.294 18.540 46.246 1.000 41.309  ? 15  GLN   AAA N   1 ? 
ATOM   93   C  CA  . GLN   A 1 16  ? -15.163 18.367 47.446 1.000 46.692  ? 15  GLN   AAA CA  1 ? 
ATOM   94   C  C   . GLN   A 1 16  ? -16.321 19.379 47.501 1.000 41.871  ? 15  GLN   AAA C   1 ? 
ATOM   95   O  O   . GLN   A 1 16  ? -17.208 19.195 48.351 1.000 34.292  ? 15  GLN   AAA O   1 ? 
ATOM   96   C  CB  . GLN   A 1 16  ? -14.282 18.468 48.694 1.000 53.490  ? 15  GLN   AAA CB  1 ? 
ATOM   97   C  CG  . GLN   A 1 16  ? -13.067 17.542 48.639 1.000 70.512  ? 15  GLN   AAA CG  1 ? 
ATOM   98   C  CD  . GLN   A 1 16  ? -13.387 16.143 48.148 1.000 77.386  ? 15  GLN   AAA CD  1 ? 
ATOM   99   O  OE1 . GLN   A 1 16  ? -14.451 15.581 48.454 1.000 91.528  ? 15  GLN   AAA OE1 1 ? 
ATOM   100  N  NE2 . GLN   A 1 16  ? -12.479 15.580 47.350 1.000 69.179  ? 15  GLN   AAA NE2 1 ? 
ATOM   101  N  N   . TRP   A 1 17  ? -16.359 20.422 46.661 1.000 32.729  ? 16  TRP   AAA N   1 ? 
ATOM   102  C  CA  . TRP   A 1 17  ? -17.438 21.431 46.814 1.000 27.571  ? 16  TRP   AAA CA  1 ? 
ATOM   103  C  C   . TRP   A 1 17  ? -18.847 20.813 46.674 1.000 27.076  ? 16  TRP   AAA C   1 ? 
ATOM   104  O  O   . TRP   A 1 17  ? -19.792 21.343 47.299 1.000 27.407  ? 16  TRP   AAA O   1 ? 
ATOM   105  C  CB  . TRP   A 1 17  ? -17.225 22.580 45.825 1.000 25.645  ? 16  TRP   AAA CB  1 ? 
ATOM   106  C  CG  . TRP   A 1 17  ? -15.984 23.384 46.049 1.000 22.970  ? 16  TRP   AAA CG  1 ? 
ATOM   107  C  CD1 . TRP   A 1 17  ? -15.221 23.483 47.171 1.000 24.596  ? 16  TRP   AAA CD1 1 ? 
ATOM   108  C  CD2 . TRP   A 1 17  ? -15.455 24.356 45.123 1.000 23.757  ? 16  TRP   AAA CD2 1 ? 
ATOM   109  N  NE1 . TRP   A 1 17  ? -14.216 24.398 46.978 1.000 23.423  ? 16  TRP   AAA NE1 1 ? 
ATOM   110  C  CE2 . TRP   A 1 17  ? -14.307 24.918 45.718 1.000 23.500  ? 16  TRP   AAA CE2 1 ? 
ATOM   111  C  CE3 . TRP   A 1 17  ? -15.762 24.677 43.805 1.000 23.103  ? 16  TRP   AAA CE3 1 ? 
ATOM   112  C  CZ2 . TRP   A 1 17  ? -13.545 25.910 45.075 1.000 22.330  ? 16  TRP   AAA CZ2 1 ? 
ATOM   113  C  CZ3 . TRP   A 1 17  ? -15.041 25.686 43.183 1.000 24.578  ? 16  TRP   AAA CZ3 1 ? 
ATOM   114  C  CH2 . TRP   A 1 17  ? -13.883 26.197 43.774 1.000 24.769  ? 16  TRP   AAA CH2 1 ? 
ATOM   115  N  N   . SER   A 1 18  ? -18.990 19.705 45.925 1.000 29.865  ? 17  SER   AAA N   1 ? 
ATOM   116  C  CA  . SER   A 1 18  ? -20.321 19.123 45.584 1.000 31.552  ? 17  SER   AAA CA  1 ? 
ATOM   117  C  C   . SER   A 1 18  ? -21.074 18.642 46.868 1.000 29.563  ? 17  SER   AAA C   1 ? 
ATOM   118  O  O   . SER   A 1 18  ? -22.322 18.494 46.813 1.000 36.363  ? 17  SER   AAA O   1 ? 
ATOM   119  C  CB  . SER   A 1 18  ? -20.178 17.992 44.584 1.000 36.095  ? 17  SER   AAA CB  1 ? 
ATOM   120  O  OG  . SER   A 1 18  ? -19.406 16.949 45.167 1.000 34.973  ? 17  SER   AAA OG  1 ? 
ATOM   121  N  N   . LYS   A 1 19  ? -20.331 18.422 47.969 1.000 29.446  ? 18  LYS   AAA N   1 ? 
ATOM   122  C  CA  . LYS   A 1 19  ? -20.884 17.934 49.273 1.000 33.151  ? 18  LYS   AAA CA  1 ? 
ATOM   123  C  C   . LYS   A 1 19  ? -21.835 18.954 49.906 1.000 38.072  ? 18  LYS   AAA C   1 ? 
ATOM   124  O  O   . LYS   A 1 19  ? -22.955 18.537 50.282 1.000 41.433  ? 18  LYS   AAA O   1 ? 
ATOM   125  C  CB  . LYS   A 1 19  ? -19.755 17.500 50.218 1.000 38.184  ? 18  LYS   AAA CB  1 ? 
ATOM   126  C  CG  . LYS   A 1 19  ? -18.965 16.317 49.679 1.000 50.358  ? 18  LYS   AAA CG  1 ? 
ATOM   127  C  CD  . LYS   A 1 19  ? -17.832 15.891 50.576 1.000 60.951  ? 18  LYS   AAA CD  1 ? 
ATOM   128  C  CE  . LYS   A 1 19  ? -16.978 14.807 49.966 1.000 66.026  ? 18  LYS   AAA CE  1 ? 
ATOM   129  N  NZ  . LYS   A 1 19  ? -15.626 14.810 50.572 1.000 75.884  ? 18  LYS   AAA NZ  1 ? 
ATOM   130  N  N   . LEU   A 1 20  ? -21.481 20.259 49.962 1.000 35.649  ? 19  LEU   AAA N   1 ? 
ATOM   131  C  CA  . LEU   A 1 20  ? -22.464 21.223 50.519 1.000 38.206  ? 19  LEU   AAA CA  1 ? 
ATOM   132  C  C   . LEU   A 1 20  ? -23.091 22.054 49.394 1.000 34.838  ? 19  LEU   AAA C   1 ? 
ATOM   133  O  O   . LEU   A 1 20  ? -24.153 22.671 49.660 1.000 35.424  ? 19  LEU   AAA O   1 ? 
ATOM   134  C  CB  . LEU   A 1 20  ? -21.847 22.133 51.589 1.000 44.038  ? 19  LEU   AAA CB  1 ? 
ATOM   135  C  CG  . LEU   A 1 20  ? -22.831 22.459 52.721 1.000 61.629  ? 19  LEU   AAA CG  1 ? 
ATOM   136  C  CD1 . LEU   A 1 20  ? -22.661 21.456 53.861 1.000 63.318  ? 19  LEU   AAA CD1 1 ? 
ATOM   137  C  CD2 . LEU   A 1 20  ? -22.716 23.900 53.223 1.000 57.296  ? 19  LEU   AAA CD2 1 ? 
ATOM   138  N  N   . TYR   A 1 21  ? -22.503 22.028 48.193 1.000 33.768  ? 20  TYR   AAA N   1 ? 
ATOM   139  C  CA  . TYR   A 1 21  ? -23.000 22.799 46.992 1.000 28.547  ? 20  TYR   AAA CA  1 ? 
ATOM   140  C  C   . TYR   A 1 21  ? -23.208 21.851 45.806 1.000 31.457  ? 20  TYR   AAA C   1 ? 
ATOM   141  O  O   . TYR   A 1 21  ? -22.323 21.786 44.891 1.000 32.744  ? 20  TYR   AAA O   1 ? 
ATOM   142  C  CB  . TYR   A 1 21  ? -22.016 23.920 46.627 1.000 26.034  ? 20  TYR   AAA CB  1 ? 
ATOM   143  C  CG  . TYR   A 1 21  ? -21.781 24.850 47.787 1.000 25.151  ? 20  TYR   AAA CG  1 ? 
ATOM   144  C  CD1 . TYR   A 1 21  ? -22.685 25.874 48.102 1.000 29.146  ? 20  TYR   AAA CD1 1 ? 
ATOM   145  C  CD2 . TYR   A 1 21  ? -20.657 24.730 48.579 1.000 28.359  ? 20  TYR   AAA CD2 1 ? 
ATOM   146  C  CE1 . TYR   A 1 21  ? -22.510 26.661 49.224 1.000 31.446  ? 20  TYR   AAA CE1 1 ? 
ATOM   147  C  CE2 . TYR   A 1 21  ? -20.469 25.521 49.703 1.000 33.540  ? 20  TYR   AAA CE2 1 ? 
ATOM   148  C  CZ  . TYR   A 1 21  ? -21.388 26.501 50.019 1.000 31.591  ? 20  TYR   AAA CZ  1 ? 
ATOM   149  O  OH  . TYR   A 1 21  ? -21.177 27.279 51.123 1.000 37.786  ? 20  TYR   AAA OH  1 ? 
ATOM   150  N  N   . PRO   A 1 22  ? -24.339 21.094 45.805 1.000 31.193  ? 21  PRO   AAA N   1 ? 
ATOM   151  C  CA  . PRO   A 1 22  ? -24.530 20.053 44.776 1.000 30.251  ? 21  PRO   AAA CA  1 ? 
ATOM   152  C  C   . PRO   A 1 22  ? -24.645 20.625 43.356 1.000 27.504  ? 21  PRO   AAA C   1 ? 
ATOM   153  O  O   . PRO   A 1 22  ? -24.432 19.934 42.385 1.000 31.687  ? 21  PRO   AAA O   1 ? 
ATOM   154  C  CB  . PRO   A 1 22  ? -25.879 19.427 45.164 1.000 35.361  ? 21  PRO   AAA CB  1 ? 
ATOM   155  C  CG  . PRO   A 1 22  ? -25.959 19.647 46.660 1.000 33.683  ? 21  PRO   AAA CG  1 ? 
ATOM   156  C  CD  . PRO   A 1 22  ? -25.336 21.010 46.887 1.000 34.629  ? 21  PRO   AAA CD  1 ? 
ATOM   157  N  N   . ILE   A 1 23  ? -24.871 21.965 43.263 1.000 29.500  ? 22  ILE   AAA N   1 ? 
ATOM   158  C  CA  . ILE   A 1 23  ? -24.934 22.622 41.933 1.000 27.327  ? 22  ILE   AAA CA  1 ? 
ATOM   159  C  C   . ILE   A 1 23  ? -23.532 22.509 41.255 1.000 24.490  ? 22  ILE   AAA C   1 ? 
ATOM   160  O  O   . ILE   A 1 23  ? -23.461 22.698 40.043 1.000 28.136  ? 22  ILE   AAA O   1 ? 
ATOM   161  C  CB  . ILE   A 1 23  ? -25.400 24.093 42.084 1.000 26.566  ? 22  ILE   AAA CB  1 ? 
ATOM   162  C  CG1 . ILE   A 1 23  ? -25.941 24.600 40.743 1.000 29.551  ? 22  ILE   AAA CG1 1 ? 
ATOM   163  C  CG2 . ILE   A 1 23  ? -24.274 24.986 42.639 1.000 27.921  ? 22  ILE   AAA CG2 1 ? 
ATOM   164  C  CD1 . ILE   A 1 23  ? -27.118 23.789 40.180 1.000 32.470  ? 22  ILE   AAA CD1 1 ? 
ATOM   165  N  N   . ALA   A 1 24  ? -22.482 22.157 42.030 1.000 26.677  ? 23  ALA   AAA N   1 ? 
ATOM   166  C  CA  . ALA   A 1 24  ? -21.112 21.983 41.499 1.000 26.925  ? 23  ALA   AAA CA  1 ? 
ATOM   167  C  C   . ALA   A 1 24  ? -21.195 21.007 40.330 1.000 24.944  ? 23  ALA   AAA C   1 ? 
ATOM   168  O  O   . ALA   A 1 24  ? -20.356 21.128 39.440 1.000 28.578  ? 23  ALA   AAA O   1 ? 
ATOM   169  C  CB  . ALA   A 1 24  ? -20.194 21.487 42.573 1.000 25.735  ? 23  ALA   AAA CB  1 ? 
ATOM   170  N  N   . ASN   A 1 25  ? -22.137 20.060 40.388 1.000 30.045  ? 24  ASN   AAA N   1 ? 
ATOM   171  C  CA  . ASN   A 1 25  ? -22.247 19.015 39.327 1.000 32.949  ? 24  ASN   AAA CA  1 ? 
ATOM   172  C  C   . ASN   A 1 25  ? -23.349 19.398 38.330 1.000 32.005  ? 24  ASN   AAA C   1 ? 
ATOM   173  O  O   . ASN   A 1 25  ? -23.745 18.536 37.559 1.000 35.663  ? 24  ASN   AAA O   1 ? 
ATOM   174  C  CB  . ASN   A 1 25  ? -22.439 17.610 39.928 1.000 33.693  ? 24  ASN   AAA CB  1 ? 
ATOM   175  C  CG  . ASN   A 1 25  ? -21.202 17.170 40.751 1.000 34.754  ? 24  ASN   AAA CG  1 ? 
ATOM   176  O  OD1 . ASN   A 1 25  ? -21.332 16.689 41.907 1.000 45.972  ? 24  ASN   AAA OD1 1 ? 
ATOM   177  N  ND2 . ASN   A 1 25  ? -19.987 17.410 40.192 1.000 36.577  ? 24  ASN   AAA ND2 1 ? 
ATOM   178  N  N   . GLY   A 1 26  ? -23.764 20.675 38.282 1.000 33.231  ? 25  GLY   AAA N   1 ? 
ATOM   179  C  CA  . GLY   A 1 26  ? -24.891 21.098 37.433 1.000 32.201  ? 25  GLY   AAA CA  1 ? 
ATOM   180  C  C   . GLY   A 1 26  ? -24.528 21.173 35.958 1.000 33.272  ? 25  GLY   AAA C   1 ? 
ATOM   181  O  O   . GLY   A 1 26  ? -23.355 20.844 35.572 1.000 31.293  ? 25  GLY   AAA O   1 ? 
ATOM   182  N  N   . ASN   A 1 27  ? -25.479 21.693 35.163 1.000 28.849  ? 26  ASN   AAA N   1 ? 
ATOM   183  C  CA  . ASN   A 1 27  ? -25.391 21.756 33.685 1.000 31.852  ? 26  ASN   AAA CA  1 ? 
ATOM   184  C  C   . ASN   A 1 27  ? -24.871 23.120 33.196 1.000 27.996  ? 26  ASN   AAA C   1 ? 
ATOM   185  O  O   . ASN   A 1 27  ? -24.697 23.238 31.945 1.000 29.926  ? 26  ASN   AAA O   1 ? 
ATOM   186  C  CB  . ASN   A 1 27  ? -26.757 21.443 33.084 1.000 36.674  ? 26  ASN   AAA CB  1 ? 
ATOM   187  C  CG  . ASN   A 1 27  ? -27.211 20.036 33.421 1.000 41.957  ? 26  ASN   AAA CG  1 ? 
ATOM   188  O  OD1 . ASN   A 1 27  ? -26.428 19.080 33.388 1.000 44.639  ? 26  ASN   AAA OD1 1 ? 
ATOM   189  N  ND2 . ASN   A 1 27  ? -28.480 19.906 33.761 1.000 47.209  ? 26  ASN   AAA ND2 1 ? 
ATOM   190  N  N   . ASN   A 1 28  ? -24.646 24.117 34.083 1.000 26.615  ? 27  ASN   AAA N   1 ? 
ATOM   191  C  CA  . ASN   A 1 28  ? -24.190 25.460 33.650 1.000 26.391  ? 27  ASN   AAA CA  1 ? 
ATOM   192  C  C   . ASN   A 1 28  ? -23.031 25.862 34.542 1.000 23.304  ? 27  ASN   AAA C   1 ? 
ATOM   193  O  O   . ASN   A 1 28  ? -22.976 27.028 34.919 1.000 24.309  ? 27  ASN   AAA O   1 ? 
ATOM   194  C  CB  . ASN   A 1 28  ? -25.346 26.476 33.672 1.000 25.675  ? 27  ASN   AAA CB  1 ? 
ATOM   195  C  CG  . ASN   A 1 28  ? -26.527 26.018 32.833 1.000 27.115  ? 27  ASN   AAA CG  1 ? 
ATOM   196  O  OD1 . ASN   A 1 28  ? -26.535 26.158 31.613 1.000 35.007  ? 27  ASN   AAA OD1 1 ? 
ATOM   197  N  ND2 . ASN   A 1 28  ? -27.553 25.479 33.464 1.000 27.619  ? 27  ASN   AAA ND2 1 ? 
ATOM   198  N  N   . GLN   A 1 29  ? -22.076 24.968 34.783 1.000 24.933  ? 28  GLN   AAA N   1 ? 
ATOM   199  C  CA  . GLN   A 1 29  ? -20.930 25.275 35.664 1.000 24.850  ? 28  GLN   AAA CA  1 ? 
ATOM   200  C  C   . GLN   A 1 29  ? -19.792 25.919 34.871 1.000 19.277  ? 28  GLN   AAA C   1 ? 
ATOM   201  O  O   . GLN   A 1 29  ? -19.665 25.711 33.659 1.000 22.695  ? 28  GLN   AAA O   1 ? 
ATOM   202  C  CB  . GLN   A 1 29  ? -20.468 24.036 36.416 1.000 24.548  ? 28  GLN   AAA CB  1 ? 
ATOM   203  C  CG  . GLN   A 1 29  ? -21.465 23.619 37.486 1.000 25.371  ? 28  GLN   AAA CG  1 ? 
ATOM   204  C  CD  . GLN   A 1 29  ? -21.506 24.668 38.571 1.000 21.348  ? 28  GLN   AAA CD  1 ? 
ATOM   205  O  OE1 . GLN   A 1 29  ? -20.540 24.780 39.337 1.000 22.930  ? 28  GLN   AAA OE1 1 ? 
ATOM   206  N  NE2 . GLN   A 1 29  ? -22.632 25.390 38.656 1.000 22.696  ? 28  GLN   AAA NE2 1 ? 
ATOM   207  N  N   . SER   A 1 30  ? -19.058 26.791 35.556 1.000 20.796  ? 29  SER   AAA N   1 ? 
ATOM   208  C  CA  . SER   A 1 30  ? -17.885 27.492 34.992 1.000 23.519  ? 29  SER   AAA CA  1 ? 
ATOM   209  C  C   . SER   A 1 30  ? -16.680 27.203 35.895 1.000 26.728  ? 29  SER   AAA C   1 ? 
ATOM   210  O  O   . SER   A 1 30  ? -16.831 26.926 37.131 1.000 24.358  ? 29  SER   AAA O   1 ? 
ATOM   211  C  CB  . SER   A 1 30  ? -18.178 29.001 34.966 1.000 20.606  ? 29  SER   AAA CB  1 ? 
ATOM   212  O  OG  . SER   A 1 30  ? -19.288 29.264 34.134 1.000 19.697  ? 29  SER   AAA OG  1 ? 
ATOM   213  N  N   . PRO   A 1 31  ? -15.446 27.335 35.330 1.000 26.285  ? 30  PRO   AAA N   1 ? 
ATOM   214  C  CA  . PRO   A 1 31  ? -15.202 27.761 33.949 1.000 23.073  ? 30  PRO   AAA CA  1 ? 
ATOM   215  C  C   . PRO   A 1 31  ? -15.260 26.622 32.943 1.000 19.578  ? 30  PRO   AAA C   1 ? 
ATOM   216  O  O   . PRO   A 1 31  ? -15.630 25.558 33.345 1.000 22.874  ? 30  PRO   AAA O   1 ? 
ATOM   217  C  CB  . PRO   A 1 31  ? -13.756 28.257 34.041 1.000 20.555  ? 30  PRO   AAA CB  1 ? 
ATOM   218  C  CG  . PRO   A 1 31  ? -13.133 27.273 35.021 1.000 22.096  ? 30  PRO   AAA CG  1 ? 
ATOM   219  C  CD  . PRO   A 1 31  ? -14.190 27.162 36.084 1.000 25.771  ? 30  PRO   AAA CD  1 ? 
ATOM   220  N  N   . VAL   A 1 32  ? -15.032 26.930 31.686 1.000 19.687  ? 31  VAL   AAA N   1 ? 
ATOM   221  C  CA  . VAL   A 1 32  ? -15.032 25.925 30.600 1.000 23.236  ? 31  VAL   AAA CA  1 ? 
ATOM   222  C  C   . VAL   A 1 32  ? -13.793 26.123 29.744 1.000 21.605  ? 31  VAL   AAA C   1 ? 
ATOM   223  O  O   . VAL   A 1 32  ? -13.130 27.182 29.845 1.000 22.043  ? 31  VAL   AAA O   1 ? 
ATOM   224  C  CB  . VAL   A 1 32  ? -16.328 26.021 29.787 1.000 23.769  ? 31  VAL   AAA CB  1 ? 
ATOM   225  C  CG1 . VAL   A 1 32  ? -17.488 25.717 30.708 1.000 23.719  ? 31  VAL   AAA CG1 1 ? 
ATOM   226  C  CG2 . VAL   A 1 32  ? -16.487 27.382 29.094 1.000 21.936  ? 31  VAL   AAA CG2 1 ? 
ATOM   227  N  N   . ASP   A 1 33  ? -13.514 25.090 28.958 1.000 22.472  ? 32  ASP   AAA N   1 ? 
ATOM   228  C  CA  . ASP   A 1 33  ? -12.524 25.076 27.877 1.000 24.121  ? 32  ASP   AAA CA  1 ? 
ATOM   229  C  C   . ASP   A 1 33  ? -13.279 25.559 26.651 1.000 23.118  ? 32  ASP   AAA C   1 ? 
ATOM   230  O  O   . ASP   A 1 33  ? -14.322 24.979 26.343 1.000 28.482  ? 32  ASP   AAA O   1 ? 
ATOM   231  C  CB  . ASP   A 1 33  ? -11.864 23.711 27.665 1.000 24.856  ? 32  ASP   AAA CB  1 ? 
ATOM   232  C  CG  . ASP   A 1 33  ? -10.900 23.773 26.496 1.000 25.510  ? 32  ASP   AAA CG  1 ? 
ATOM   233  O  OD1 . ASP   A 1 33  ? -10.018 24.663 26.492 1.000 24.853  ? 32  ASP   AAA OD1 1 ? 
ATOM   234  O  OD2 . ASP   A 1 33  ? -11.047 22.963 25.585 1.000 28.429  ? 32  ASP   AAA OD2 1 ? 
ATOM   235  N  N   . ILE   A 1 34  ? -12.889 26.718 26.117 1.000 22.890  ? 33  ILE   AAA N   1 ? 
ATOM   236  C  CA  . ILE   A 1 34  ? -13.457 27.217 24.834 1.000 22.495  ? 33  ILE   AAA CA  1 ? 
ATOM   237  C  C   . ILE   A 1 34  ? -12.751 26.501 23.671 1.000 24.473  ? 33  ILE   AAA C   1 ? 
ATOM   238  O  O   . ILE   A 1 34  ? -11.533 26.798 23.406 1.000 25.467  ? 33  ILE   AAA O   1 ? 
ATOM   239  C  CB  . ILE   A 1 34  ? -13.358 28.761 24.773 1.000 22.163  ? 33  ILE   AAA CB  1 ? 
ATOM   240  C  CG1 . ILE   A 1 34  ? -14.179 29.387 25.896 1.000 21.244  ? 33  ILE   AAA CG1 1 ? 
ATOM   241  C  CG2 . ILE   A 1 34  ? -13.800 29.271 23.411 1.000 23.682  ? 33  ILE   AAA CG2 1 ? 
ATOM   242  C  CD1 . ILE   A 1 34  ? -14.063 30.891 25.992 1.000 25.354  ? 33  ILE   AAA CD1 1 ? 
ATOM   243  N  N   . LYS   A 1 35  ? -13.452 25.559 23.022 1.000 25.980  ? 34  LYS   AAA N   1 ? 
ATOM   244  C  CA  . LYS   A 1 35  ? -12.953 24.973 21.755 1.000 25.711  ? 34  LYS   AAA CA  1 ? 
ATOM   245  C  C   . LYS   A 1 35  ? -13.386 25.853 20.577 1.000 26.654  ? 34  LYS   AAA C   1 ? 
ATOM   246  O  O   . LYS   A 1 35  ? -14.589 25.916 20.295 1.000 30.330  ? 34  LYS   AAA O   1 ? 
ATOM   247  C  CB  . LYS   A 1 35  ? -13.424 23.525 21.622 1.000 29.858  ? 34  LYS   AAA CB  1 ? 
ATOM   248  C  CG  . LYS   A 1 35  ? -12.990 22.652 22.783 1.000 33.506  ? 34  LYS   AAA CG  1 ? 
ATOM   249  C  CD  . LYS   A 1 35  ? -13.507 21.213 22.734 1.000 43.660  ? 34  LYS   AAA CD  1 ? 
ATOM   250  C  CE  . LYS   A 1 35  ? -12.857 20.297 23.762 1.000 49.623  ? 34  LYS   AAA CE  1 ? 
ATOM   251  N  NZ  . LYS   A 1 35  ? -12.766 20.912 25.116 1.000 44.678  ? 34  LYS   AAA NZ  1 ? 
ATOM   252  N  N   . THR   A 1 36  ? -12.429 26.499 19.906 1.000 24.995  ? 35  THR   AAA N   1 ? 
ATOM   253  C  CA  . THR   A 1 36  ? -12.739 27.549 18.899 1.000 27.968  ? 35  THR   AAA CA  1 ? 
ATOM   254  C  C   . THR   A 1 36  ? -13.362 26.964 17.635 1.000 27.492  ? 35  THR   AAA C   1 ? 
ATOM   255  O  O   . THR   A 1 36  ? -14.042 27.723 16.938 1.000 33.655  ? 35  THR   AAA O   1 ? 
ATOM   256  C  CB  . THR   A 1 36  ? -11.514 28.403 18.565 1.000 29.600  ? 35  THR   AAA CB  1 ? 
ATOM   257  O  OG1 . THR   A 1 36  ? -10.423 27.566 18.194 1.000 27.950  ? 35  THR   AAA OG1 1 ? 
ATOM   258  C  CG2 . THR   A 1 36  ? -11.102 29.276 19.728 1.000 33.923  ? 35  THR   AAA CG2 1 ? 
ATOM   259  N  N   . SER   A 1 37  ? -13.169 25.676 17.346 1.000 33.526  ? 36  SER   AAA N   1 ? 
ATOM   260  C  CA  . SER   A 1 37  ? -13.785 24.982 16.180 1.000 34.316  ? 36  SER   AAA CA  1 ? 
ATOM   261  C  C   . SER   A 1 37  ? -15.261 24.666 16.452 1.000 31.695  ? 36  SER   AAA C   1 ? 
ATOM   262  O  O   . SER   A 1 37  ? -15.954 24.292 15.499 1.000 42.871  ? 36  SER   AAA O   1 ? 
ATOM   263  C  CB  . SER   A 1 37  ? -13.036 23.731 15.853 1.000 36.224  ? 36  SER   AAA CB  1 ? 
ATOM   264  O  OG  . SER   A 1 37  ? -13.162 22.815 16.932 1.000 41.044  ? 36  SER   AAA OG  1 ? 
ATOM   265  N  N   . GLU   A 1 38  ? -15.712 24.789 17.705 1.000 30.121  ? 37  GLU   AAA N   1 ? 
ATOM   266  C  CA  . GLU   A 1 38  ? -17.100 24.501 18.134 1.000 32.826  ? 37  GLU   AAA CA  1 ? 
ATOM   267  C  C   . GLU   A 1 38  ? -17.854 25.809 18.485 1.000 32.963  ? 37  GLU   AAA C   1 ? 
ATOM   268  O  O   . GLU   A 1 38  ? -19.066 25.726 18.745 1.000 34.546  ? 37  GLU   AAA O   1 ? 
ATOM   269  C  CB  . GLU   A 1 38  ? -17.026 23.476 19.273 1.000 33.226  ? 37  GLU   AAA CB  1 ? 
ATOM   270  C  CG  . GLU   A 1 38  ? -16.356 22.158 18.847 1.000 41.256  ? 37  GLU   AAA CG  1 ? 
ATOM   271  C  CD  . GLU   A 1 38  ? -16.414 21.006 19.845 1.000 51.560  ? 37  GLU   AAA CD  1 ? 
ATOM   272  O  OE1 . GLU   A 1 38  ? -16.964 21.218 20.941 1.000 59.574  ? 37  GLU   AAA OE1 1 ? 
ATOM   273  O  OE2 . GLU   A 1 38  ? -15.913 19.882 19.525 1.000 73.355  ? 37  GLU   AAA OE2 1 ? 
ATOM   274  N  N   . THR   A 1 39  ? -17.225 26.991 18.480 1.000 31.392  ? 38  THR   AAA N   1 ? 
ATOM   275  C  CA  . THR   A 1 39  ? -17.937 28.261 18.759 1.000 32.745  ? 38  THR   AAA CA  1 ? 
ATOM   276  C  C   . THR   A 1 39  ? -18.862 28.610 17.585 1.000 36.311  ? 38  THR   AAA C   1 ? 
ATOM   277  O  O   . THR   A 1 39  ? -18.566 28.231 16.444 1.000 36.927  ? 38  THR   AAA O   1 ? 
ATOM   278  C  CB  . THR   A 1 39  ? -16.943 29.388 19.062 1.000 30.668  ? 38  THR   AAA CB  1 ? 
ATOM   279  O  OG1 . THR   A 1 39  ? -16.060 29.555 17.954 1.000 29.840  ? 38  THR   AAA OG1 1 ? 
ATOM   280  C  CG2 . THR   A 1 39  ? -16.146 29.095 20.315 1.000 29.288  ? 38  THR   AAA CG2 1 ? 
ATOM   281  N  N   . LYS   A 1 40  ? -19.956 29.320 17.850 1.000 33.503  ? 39  LYS   AAA N   1 ? 
ATOM   282  C  CA  . LYS   A 1 40  ? -20.894 29.731 16.780 1.000 35.613  ? 39  LYS   AAA CA  1 ? 
ATOM   283  C  C   . LYS   A 1 40  ? -20.843 31.245 16.685 1.000 33.971  ? 39  LYS   AAA C   1 ? 
ATOM   284  O  O   . LYS   A 1 40  ? -21.159 31.887 17.715 1.000 35.980  ? 39  LYS   AAA O   1 ? 
ATOM   285  C  CB  . LYS   A 1 40  ? -22.308 29.219 17.063 1.000 44.566  ? 39  LYS   AAA CB  1 ? 
ATOM   286  C  CG  . LYS   A 1 40  ? -22.512 27.757 16.698 1.000 59.511  ? 39  LYS   AAA CG  1 ? 
ATOM   287  C  CD  . LYS   A 1 40  ? -23.955 27.367 16.437 1.000 62.593  ? 39  LYS   AAA CD  1 ? 
ATOM   288  C  CE  . LYS   A 1 40  ? -24.174 25.869 16.495 1.000 69.331  ? 39  LYS   AAA CE  1 ? 
ATOM   289  N  NZ  . LYS   A 1 40  ? -25.527 25.554 17.004 1.000 73.742  ? 39  LYS   AAA NZ  1 ? 
ATOM   290  N  N   . HIS   A 1 41  ? -20.415 31.784 15.542 1.000 31.502  ? 40  HIS   AAA N   1 ? 
ATOM   291  C  CA  . HIS   A 1 41  ? -20.426 33.257 15.331 1.000 36.566  ? 40  HIS   AAA CA  1 ? 
ATOM   292  C  C   . HIS   A 1 41  ? -21.889 33.709 15.390 1.000 40.615  ? 40  HIS   AAA C   1 ? 
ATOM   293  O  O   . HIS   A 1 41  ? -22.738 33.090 14.707 1.000 47.352  ? 40  HIS   AAA O   1 ? 
ATOM   294  C  CB  . HIS   A 1 41  ? -19.733 33.689 14.030 1.000 41.015  ? 40  HIS   AAA CB  1 ? 
ATOM   295  C  CG  . HIS   A 1 41  ? -19.815 35.167 13.805 1.000 42.320  ? 40  HIS   AAA CG  1 ? 
ATOM   296  N  ND1 . HIS   A 1 41  ? -19.069 36.075 14.536 1.000 50.675  ? 40  HIS   AAA ND1 1 ? 
ATOM   297  C  CD2 . HIS   A 1 41  ? -20.567 35.904 12.964 1.000 47.019  ? 40  HIS   AAA CD2 1 ? 
ATOM   298  C  CE1 . HIS   A 1 41  ? -19.342 37.299 14.139 1.000 49.262  ? 40  HIS   AAA CE1 1 ? 
ATOM   299  N  NE2 . HIS   A 1 41  ? -20.256 37.223 13.184 1.000 53.379  ? 40  HIS   AAA NE2 1 ? 
ATOM   300  N  N   . ASP   A 1 42  ? -22.181 34.713 16.215 1.000 44.076  ? 41  ASP   AAA N   1 ? 
ATOM   301  C  CA  . ASP   A 1 42  ? -23.553 35.251 16.376 1.000 43.341  ? 41  ASP   AAA CA  1 ? 
ATOM   302  C  C   . ASP   A 1 42  ? -23.581 36.721 15.956 1.000 46.331  ? 41  ASP   AAA C   1 ? 
ATOM   303  O  O   . ASP   A 1 42  ? -23.043 37.579 16.694 1.000 45.134  ? 41  ASP   AAA O   1 ? 
ATOM   304  C  CB  . ASP   A 1 42  ? -24.083 35.046 17.790 1.000 42.253  ? 41  ASP   AAA CB  1 ? 
ATOM   305  C  CG  . ASP   A 1 42  ? -25.533 35.470 17.919 1.000 40.459  ? 41  ASP   AAA CG  1 ? 
ATOM   306  O  OD1 . ASP   A 1 42  ? -26.068 36.073 16.957 1.000 49.147  ? 41  ASP   AAA OD1 1 ? 
ATOM   307  O  OD2 . ASP   A 1 42  ? -26.110 35.205 18.978 1.000 45.225  ? 41  ASP   AAA OD2 1 ? 
ATOM   308  N  N   . THR   A 1 43  ? -24.241 36.951 14.819 1.000 46.417  ? 42  THR   AAA N   1 ? 
ATOM   309  C  CA  . THR   A 1 43  ? -24.433 38.238 14.101 1.000 47.570  ? 42  THR   AAA CA  1 ? 
ATOM   310  C  C   . THR   A 1 43  ? -25.142 39.266 14.995 1.000 50.669  ? 42  THR   AAA C   1 ? 
ATOM   311  O  O   . THR   A 1 43  ? -24.873 40.473 14.811 1.000 49.860  ? 42  THR   AAA O   1 ? 
ATOM   312  C  CB  . THR   A 1 43  ? -25.203 37.977 12.798 1.000 55.191  ? 42  THR   AAA CB  1 ? 
ATOM   313  O  OG1 . THR   A 1 43  ? -25.243 39.204 12.085 1.000 67.476  ? 42  THR   AAA OG1 1 ? 
ATOM   314  C  CG2 . THR   A 1 43  ? -26.621 37.480 12.995 1.000 62.543  ? 42  THR   AAA CG2 1 ? 
ATOM   315  N  N   . SER   A 1 44  ? -26.017 38.832 15.910 1.000 45.317  ? 43  SER   AAA N   1 ? 
ATOM   316  C  CA  . SER   A 1 44  ? -26.848 39.732 16.759 1.000 45.617  ? 43  SER   AAA CA  1 ? 
ATOM   317  C  C   . SER   A 1 44  ? -26.054 40.291 17.952 1.000 42.696  ? 43  SER   AAA C   1 ? 
ATOM   318  O  O   . SER   A 1 44  ? -26.535 41.277 18.558 1.000 47.100  ? 43  SER   AAA O   1 ? 
ATOM   319  C  CB  . SER   A 1 44  ? -28.089 39.043 17.225 1.000 47.650  ? 43  SER   AAA CB  1 ? 
ATOM   320  O  OG  . SER   A 1 44  ? -27.772 38.059 18.204 1.000 39.622  ? 43  SER   AAA OG  1 ? 
ATOM   321  N  N   . LEU   A 1 45  ? -24.899 39.711 18.306 1.000 37.062  ? 44  LEU   AAA N   1 ? 
ATOM   322  C  CA  . LEU   A 1 45  ? -24.075 40.235 19.429 1.000 34.038  ? 44  LEU   AAA CA  1 ? 
ATOM   323  C  C   . LEU   A 1 45  ? -23.598 41.651 19.111 1.000 35.249  ? 44  LEU   AAA C   1 ? 
ATOM   324  O  O   . LEU   A 1 45  ? -22.990 41.874 18.056 1.000 35.080  ? 44  LEU   AAA O   1 ? 
ATOM   325  C  CB  . LEU   A 1 45  ? -22.880 39.320 19.710 1.000 32.940  ? 44  LEU   AAA CB  1 ? 
ATOM   326  C  CG  . LEU   A 1 45  ? -23.206 37.950 20.302 1.000 27.770  ? 44  LEU   AAA CG  1 ? 
ATOM   327  C  CD1 . LEU   A 1 45  ? -21.912 37.189 20.424 1.000 29.065  ? 44  LEU   AAA CD1 1 ? 
ATOM   328  C  CD2 . LEU   A 1 45  ? -23.860 38.065 21.668 1.000 30.510  ? 44  LEU   AAA CD2 1 ? 
ATOM   329  N  N   . LYS   A 1 46  ? -23.867 42.575 20.022 1.000 34.426  ? 45  LYS   AAA N   1 ? 
ATOM   330  C  CA  . LYS   A 1 46  ? -23.428 43.979 19.865 1.000 36.021  ? 45  LYS   AAA CA  1 ? 
ATOM   331  C  C   . LYS   A 1 46  ? -22.072 44.111 20.543 1.000 33.320  ? 45  LYS   AAA C   1 ? 
ATOM   332  O  O   . LYS   A 1 46  ? -21.633 43.217 21.288 1.000 34.452  ? 45  LYS   AAA O   1 ? 
ATOM   333  C  CB  . LYS   A 1 46  ? -24.545 44.913 20.338 1.000 41.735  ? 45  LYS   AAA CB  1 ? 
ATOM   334  C  CG  . LYS   A 1 46  ? -25.801 44.801 19.474 1.000 50.545  ? 45  LYS   AAA CG  1 ? 
ATOM   335  C  CD  . LYS   A 1 46  ? -26.768 45.956 19.572 1.000 59.709  ? 45  LYS   AAA CD  1 ? 
ATOM   336  C  CE  . LYS   A 1 46  ? -27.962 45.788 18.651 1.000 62.902  ? 45  LYS   AAA CE  1 ? 
ATOM   337  N  NZ  . LYS   A 1 46  ? -28.694 44.532 18.949 1.000 73.598  ? 45  LYS   AAA NZ  1 ? 
ATOM   338  N  N   . PRO   A 1 47  ? -21.319 45.189 20.234 1.000 34.326  ? 46  PRO   AAA N   1 ? 
ATOM   339  C  CA  . PRO   A 1 47  ? -20.074 45.445 20.939 1.000 34.210  ? 46  PRO   AAA CA  1 ? 
ATOM   340  C  C   . PRO   A 1 47  ? -20.368 45.579 22.443 1.000 29.364  ? 46  PRO   AAA C   1 ? 
ATOM   341  O  O   . PRO   A 1 47  ? -21.455 45.970 22.815 1.000 32.921  ? 46  PRO   AAA O   1 ? 
ATOM   342  C  CB  . PRO   A 1 47  ? -19.530 46.731 20.288 1.000 37.019  ? 46  PRO   AAA CB  1 ? 
ATOM   343  C  CG  . PRO   A 1 47  ? -20.253 46.845 18.953 1.000 34.818  ? 46  PRO   AAA CG  1 ? 
ATOM   344  C  CD  . PRO   A 1 47  ? -21.597 46.181 19.183 1.000 36.625  ? 46  PRO   AAA CD  1 ? 
ATOM   345  N  N   . ILE   A 1 48  ? -19.428 45.117 23.263 1.000 29.971  ? 47  ILE   AAA N   1 ? 
ATOM   346  C  CA  . ILE   A 1 48  ? -19.378 45.387 24.726 1.000 28.425  ? 47  ILE   AAA CA  1 ? 
ATOM   347  C  C   . ILE   A 1 48  ? -19.075 46.867 24.927 1.000 24.900  ? 47  ILE   AAA C   1 ? 
ATOM   348  O  O   . ILE   A 1 48  ? -18.093 47.339 24.331 1.000 31.142  ? 47  ILE   AAA O   1 ? 
ATOM   349  C  CB  . ILE   A 1 48  ? -18.293 44.535 25.387 1.000 32.074  ? 47  ILE   AAA CB  1 ? 
ATOM   350  C  CG1 . ILE   A 1 48  ? -18.721 43.073 25.409 1.000 35.747  ? 47  ILE   AAA CG1 1 ? 
ATOM   351  C  CG2 . ILE   A 1 48  ? -17.942 45.070 26.768 1.000 36.257  ? 47  ILE   AAA CG2 1 ? 
ATOM   352  C  CD1 . ILE   A 1 48  ? -20.029 42.826 26.151 1.000 35.524  ? 47  ILE   AAA CD1 1 ? 
ATOM   353  N  N   . SER   A 1 49  ? -19.860 47.513 25.789 1.000 25.937  ? 48  SER   AAA N   1 ? 
ATOM   354  C  CA  . SER   A 1 49  ? -19.697 48.925 26.210 1.000 30.582  ? 48  SER   AAA CA  1 ? 
ATOM   355  C  C   . SER   A 1 49  ? -19.494 48.918 27.724 1.000 29.005  ? 48  SER   AAA C   1 ? 
ATOM   356  O  O   . SER   A 1 49  ? -20.386 48.456 28.443 1.000 30.494  ? 48  SER   AAA O   1 ? 
ATOM   357  C  CB  . SER   A 1 49  ? -20.892 49.744 25.734 1.000 40.034  ? 48  SER   AAA CB  1 ? 
ATOM   358  O  OG  . SER   A 1 49  ? -21.223 50.792 26.636 1.000 44.191  ? 48  SER   AAA OG  1 ? 
ATOM   359  N  N   . VAL   A 1 50  ? -18.326 49.347 28.189 1.000 25.960  ? 49  VAL   AAA N   1 ? 
ATOM   360  C  CA  . VAL   A 1 50  ? -18.098 49.566 29.644 1.000 27.076  ? 49  VAL   AAA CA  1 ? 
ATOM   361  C  C   . VAL   A 1 50  ? -17.934 51.066 29.858 1.000 27.108  ? 49  VAL   AAA C   1 ? 
ATOM   362  O  O   . VAL   A 1 50  ? -17.254 51.724 29.084 1.000 28.548  ? 49  VAL   AAA O   1 ? 
ATOM   363  C  CB  . VAL   A 1 50  ? -16.934 48.751 30.252 1.000 27.491  ? 49  VAL   AAA CB  1 ? 
ATOM   364  C  CG1 . VAL   A 1 50  ? -17.240 47.259 30.271 1.000 26.734  ? 49  VAL   AAA CG1 1 ? 
ATOM   365  C  CG2 . VAL   A 1 50  ? -15.606 49.020 29.576 1.000 32.499  ? 49  VAL   AAA CG2 1 ? 
ATOM   366  N  N   . SER   A 1 51  ? -18.612 51.575 30.863 1.000 27.824  ? 50  SER   AAA N   1 ? 
ATOM   367  C  CA  . SER   A 1 51  ? -18.447 52.983 31.275 1.000 27.917  ? 50  SER   AAA CA  1 ? 
ATOM   368  C  C   . SER   A 1 51  ? -18.359 52.994 32.795 1.000 25.158  ? 50  SER   AAA C   1 ? 
ATOM   369  O  O   . SER   A 1 51  ? -19.411 52.883 33.456 1.000 23.935  ? 50  SER   AAA O   1 ? 
ATOM   370  C  CB  . SER   A 1 51  ? -19.575 53.815 30.749 1.000 30.783  ? 50  SER   AAA CB  1 ? 
ATOM   371  O  OG  . SER   A 1 51  ? -19.362 55.141 31.173 1.000 37.961  ? 50  SER   AAA OG  1 ? 
ATOM   372  N  N   . TYR   A 1 52  ? -17.147 53.078 33.309 1.000 25.466  ? 51  TYR   AAA N   1 ? 
ATOM   373  C  CA  . TYR   A 1 52  ? -16.940 52.993 34.789 1.000 25.669  ? 51  TYR   AAA CA  1 ? 
ATOM   374  C  C   . TYR   A 1 52  ? -16.473 54.362 35.265 1.000 26.822  ? 51  TYR   AAA C   1 ? 
ATOM   375  O  O   . TYR   A 1 52  ? -15.621 54.975 34.616 1.000 31.496  ? 51  TYR   AAA O   1 ? 
ATOM   376  C  CB  . TYR   A 1 52  ? -15.922 51.908 35.134 1.000 25.609  ? 51  TYR   AAA CB  1 ? 
ATOM   377  C  CG  . TYR   A 1 52  ? -16.222 50.506 34.668 1.000 23.147  ? 51  TYR   AAA CG  1 ? 
ATOM   378  C  CD1 . TYR   A 1 52  ? -17.498 49.974 34.610 1.000 21.337  ? 51  TYR   AAA CD1 1 ? 
ATOM   379  C  CD2 . TYR   A 1 52  ? -15.158 49.695 34.307 1.000 20.804  ? 51  TYR   AAA CD2 1 ? 
ATOM   380  C  CE1 . TYR   A 1 52  ? -17.705 48.652 34.223 1.000 19.799  ? 51  TYR   AAA CE1 1 ? 
ATOM   381  C  CE2 . TYR   A 1 52  ? -15.350 48.370 33.948 1.000 23.340  ? 51  TYR   AAA CE2 1 ? 
ATOM   382  C  CZ  . TYR   A 1 52  ? -16.624 47.857 33.866 1.000 22.316  ? 51  TYR   AAA CZ  1 ? 
ATOM   383  O  OH  . TYR   A 1 52  ? -16.773 46.539 33.493 1.000 21.695  ? 51  TYR   AAA OH  1 ? 
ATOM   384  N  N   . ASN   A 1 53  ? -16.998 54.750 36.413 1.000 24.562  ? 52  ASN   AAA N   1 ? 
ATOM   385  C  CA  . ASN   A 1 53  ? -16.654 56.011 37.109 1.000 27.061  ? 52  ASN   AAA CA  1 ? 
ATOM   386  C  C   . ASN   A 1 53  ? -15.616 55.686 38.185 1.000 26.005  ? 52  ASN   AAA C   1 ? 
ATOM   387  O  O   . ASN   A 1 53  ? -15.933 54.922 39.132 1.000 27.375  ? 52  ASN   AAA O   1 ? 
ATOM   388  C  CB  . ASN   A 1 53  ? -17.934 56.551 37.727 1.000 27.834  ? 52  ASN   AAA CB  1 ? 
ATOM   389  C  CG  . ASN   A 1 53  ? -17.761 57.947 38.282 1.000 29.731  ? 52  ASN   AAA CG  1 ? 
ATOM   390  O  OD1 . ASN   A 1 53  ? -16.727 58.264 38.866 1.000 29.280  ? 52  ASN   AAA OD1 1 ? 
ATOM   391  N  ND2 . ASN   A 1 53  ? -18.804 58.742 38.150 1.000 31.091  ? 52  ASN   AAA ND2 1 ? 
ATOM   392  N  N   . PRO   A 1 54  ? -14.379 56.239 38.145 1.000 23.667  ? 53  PRO   AAA N   1 ? 
ATOM   393  C  CA  . PRO   A 1 54  ? -13.354 55.890 39.128 1.000 23.887  ? 53  PRO   AAA CA  1 ? 
ATOM   394  C  C   . PRO   A 1 54  ? -13.760 56.204 40.571 1.000 22.669  ? 53  PRO   AAA C   1 ? 
ATOM   395  O  O   . PRO   A 1 54  ? -13.182 55.676 41.451 1.000 24.634  ? 53  PRO   AAA O   1 ? 
ATOM   396  C  CB  . PRO   A 1 54  ? -12.121 56.697 38.671 1.000 25.254  ? 53  PRO   AAA CB  1 ? 
ATOM   397  C  CG  . PRO   A 1 54  ? -12.721 57.893 37.962 1.000 31.571  ? 53  PRO   AAA CG  1 ? 
ATOM   398  C  CD  . PRO   A 1 54  ? -13.917 57.300 37.231 1.000 27.392  ? 53  PRO   AAA CD  1 ? 
ATOM   399  N  N   . ALA   A 1 55  ? -14.737 57.122 40.774 1.000 26.525  ? 54  ALA   AAA N   1 ? 
ATOM   400  C  CA  . ALA   A 1 55  ? -15.207 57.441 42.135 1.000 25.799  ? 54  ALA   AAA CA  1 ? 
ATOM   401  C  C   . ALA   A 1 55  ? -16.056 56.313 42.732 1.000 25.735  ? 54  ALA   AAA C   1 ? 
ATOM   402  O  O   . ALA   A 1 55  ? -16.362 56.436 43.924 1.000 26.676  ? 54  ALA   AAA O   1 ? 
ATOM   403  C  CB  . ALA   A 1 55  ? -16.004 58.724 42.101 1.000 33.113  ? 54  ALA   AAA CB  1 ? 
ATOM   404  N  N   . THR   A 1 56  ? -16.419 55.267 41.967 1.000 25.056  ? 55  THR   AAA N   1 ? 
ATOM   405  C  CA  . THR   A 1 56  ? -17.191 54.127 42.549 1.000 22.775  ? 55  THR   AAA CA  1 ? 
ATOM   406  C  C   . THR   A 1 56  ? -16.245 53.150 43.249 1.000 21.018  ? 55  THR   AAA C   1 ? 
ATOM   407  O  O   . THR   A 1 56  ? -16.764 52.361 44.039 1.000 21.097  ? 55  THR   AAA O   1 ? 
ATOM   408  C  CB  . THR   A 1 56  ? -18.078 53.428 41.507 1.000 22.337  ? 55  THR   AAA CB  1 ? 
ATOM   409  O  OG1 . THR   A 1 56  ? -17.261 52.985 40.392 1.000 23.009  ? 55  THR   AAA OG1 1 ? 
ATOM   410  C  CG2 . THR   A 1 56  ? -19.169 54.343 40.984 1.000 23.883  ? 55  THR   AAA CG2 1 ? 
ATOM   411  N  N   . ALA   A 1 57  ? -14.934 53.226 43.018 1.000 20.668  ? 56  ALA   AAA N   1 ? 
ATOM   412  C  CA  . ALA   A 1 57  ? -13.967 52.308 43.691 1.000 22.300  ? 56  ALA   AAA CA  1 ? 
ATOM   413  C  C   . ALA   A 1 57  ? -14.022 52.548 45.200 1.000 22.138  ? 56  ALA   AAA C   1 ? 
ATOM   414  O  O   . ALA   A 1 57  ? -14.029 53.719 45.589 1.000 22.591  ? 56  ALA   AAA O   1 ? 
ATOM   415  C  CB  . ALA   A 1 57  ? -12.583 52.464 43.163 1.000 22.289  ? 56  ALA   AAA CB  1 ? 
ATOM   416  N  N   . LYS   A 1 58  ? -14.157 51.489 46.016 1.000 20.593  ? 57  LYS   AAA N   1 ? 
ATOM   417  C  CA  . LYS   A 1 58  ? -14.434 51.606 47.462 1.000 22.574  ? 57  LYS   AAA CA  1 ? 
ATOM   418  C  C   . LYS   A 1 58  ? -13.298 51.031 48.307 1.000 23.770  ? 57  LYS   AAA C   1 ? 
ATOM   419  O  O   . LYS   A 1 58  ? -12.672 51.742 49.123 1.000 27.287  ? 57  LYS   AAA O   1 ? 
ATOM   420  C  CB  . LYS   A 1 58  ? -15.795 50.975 47.738 1.000 27.436  ? 57  LYS   AAA CB  1 ? 
ATOM   421  C  CG  . LYS   A 1 58  ? -16.329 51.119 49.146 1.000 31.783  ? 57  LYS   AAA CG  1 ? 
ATOM   422  C  CD  . LYS   A 1 58  ? -17.534 50.210 49.323 1.000 43.904  ? 57  LYS   AAA CD  1 ? 
ATOM   423  C  CE  . LYS   A 1 58  ? -18.323 50.504 50.574 1.000 49.999  ? 57  LYS   AAA CE  1 ? 
ATOM   424  N  NZ  . LYS   A 1 58  ? -19.729 50.074 50.407 1.000 58.504  ? 57  LYS   AAA NZ  1 ? 
ATOM   425  N  N   . GLU   A 1 59  ? -13.042 49.720 48.173 1.000 19.714  ? 58  GLU   AAA N   1 ? 
ATOM   426  C  CA  . GLU   A 1 59  ? -12.328 48.981 49.227 1.000 20.290  ? 58  GLU   AAA CA  1 ? 
ATOM   427  C  C   . GLU   A 1 59  ? -11.630 47.775 48.588 1.000 17.955  ? 58  GLU   AAA C   1 ? 
ATOM   428  O  O   . GLU   A 1 59  ? -12.138 47.252 47.577 1.000 20.696  ? 58  GLU   AAA O   1 ? 
ATOM   429  C  CB  . GLU   A 1 59  ? -13.343 48.513 50.274 1.000 23.473  ? 58  GLU   AAA CB  1 ? 
ATOM   430  C  CG  . GLU   A 1 59  ? -12.707 48.031 51.552 1.000 27.346  ? 58  GLU   AAA CG  1 ? 
ATOM   431  C  CD  . GLU   A 1 59  ? -13.704 47.812 52.674 1.000 28.128  ? 58  GLU   AAA CD  1 ? 
ATOM   432  O  OE1 . GLU   A 1 59  ? -13.349 48.135 53.839 1.000 31.434  ? 58  GLU   AAA OE1 1 ? 
ATOM   433  O  OE2 . GLU   A 1 59  ? -14.804 47.229 52.388 1.000 32.169  ? 58  GLU   AAA OE2 1 ? 
ATOM   434  N  N   . ILE   A 1 60  ? -10.460 47.459 49.119 1.000 19.532  ? 59  ILE   AAA N   1 ? 
ATOM   435  C  CA  . ILE   A 1 60  ? -9.726  46.206 48.799 1.000 17.411  ? 59  ILE   AAA CA  1 ? 
ATOM   436  C  C   . ILE   A 1 60  ? -9.709  45.343 50.062 1.000 18.768  ? 59  ILE   AAA C   1 ? 
ATOM   437  O  O   . ILE   A 1 60  ? -9.454  45.845 51.176 1.000 19.460  ? 59  ILE   AAA O   1 ? 
ATOM   438  C  CB  . ILE   A 1 60  ? -8.334  46.477 48.183 1.000 18.165  ? 59  ILE   AAA CB  1 ? 
ATOM   439  C  CG1 . ILE   A 1 60  ? -7.760  45.186 47.586 1.000 19.354  ? 59  ILE   AAA CG1 1 ? 
ATOM   440  C  CG2 . ILE   A 1 60  ? -7.346  47.122 49.158 1.000 19.832  ? 59  ILE   AAA CG2 1 ? 
ATOM   441  C  CD1 . ILE   A 1 60  ? -6.503  45.334 46.836 1.000 19.225  ? 59  ILE   AAA CD1 1 ? 
ATOM   442  N  N   . ILE   A 1 61  ? -10.024 44.050 49.879 1.000 18.991  ? 60  ILE   AAA N   1 ? 
ATOM   443  C  CA  . ILE   A 1 61  ? -10.264 43.122 51.018 1.000 20.826  ? 60  ILE   AAA CA  1 ? 
ATOM   444  C  C   . ILE   A 1 61  ? -9.517  41.816 50.747 1.000 17.813  ? 60  ILE   AAA C   1 ? 
ATOM   445  O  O   . ILE   A 1 61  ? -9.604  41.302 49.597 1.000 19.121  ? 60  ILE   AAA O   1 ? 
ATOM   446  C  CB  . ILE   A 1 61  ? -11.762 42.832 51.249 1.000 20.524  ? 60  ILE   AAA CB  1 ? 
ATOM   447  C  CG1 . ILE   A 1 61  ? -12.583 44.124 51.333 1.000 26.309  ? 60  ILE   AAA CG1 1 ? 
ATOM   448  C  CG2 . ILE   A 1 61  ? -11.922 42.030 52.534 1.000 23.375  ? 60  ILE   AAA CG2 1 ? 
ATOM   449  C  CD1 . ILE   A 1 61  ? -14.074 43.929 51.305 1.000 37.062  ? 60  ILE   AAA CD1 1 ? 
ATOM   450  N  N   . ASN   A 1 62  ? -8.784  41.363 51.758 1.000 19.437  ? 61  ASN   AAA N   1 ? 
ATOM   451  C  CA  . ASN   A 1 62  ? -8.227  39.971 51.789 1.000 18.051  ? 61  ASN   AAA CA  1 ? 
ATOM   452  C  C   . ASN   A 1 62  ? -9.328  39.055 52.303 1.000 19.291  ? 61  ASN   AAA C   1 ? 
ATOM   453  O  O   . ASN   A 1 62  ? -9.647  39.113 53.514 1.000 19.438  ? 61  ASN   AAA O   1 ? 
ATOM   454  C  CB  . ASN   A 1 62  ? -6.923  39.901 52.593 1.000 19.100  ? 61  ASN   AAA CB  1 ? 
ATOM   455  C  CG  . ASN   A 1 62  ? -6.291  38.524 52.652 1.000 20.703  ? 61  ASN   AAA CG  1 ? 
ATOM   456  O  OD1 . ASN   A 1 62  ? -7.009  37.528 52.585 1.000 21.826  ? 61  ASN   AAA OD1 1 ? 
ATOM   457  N  ND2 . ASN   A 1 62  ? -4.973  38.479 52.766 1.000 20.445  ? 61  ASN   AAA ND2 1 ? 
ATOM   458  N  N   . VAL   A 1 63  ? -9.866  38.209 51.416 1.000 19.484  ? 62  VAL   AAA N   1 ? 
ATOM   459  C  CA  . VAL   A 1 63  ? -10.993 37.305 51.789 1.000 20.003  ? 62  VAL   AAA CA  1 ? 
ATOM   460  C  C   . VAL   A 1 63  ? -10.457 35.889 51.994 1.000 19.384  ? 62  VAL   AAA C   1 ? 
ATOM   461  O  O   . VAL   A 1 63  ? -11.301 34.989 51.994 1.000 24.908  ? 62  VAL   AAA O   1 ? 
ATOM   462  C  CB  . VAL   A 1 63  ? -12.150 37.353 50.763 1.000 20.576  ? 62  VAL   AAA CB  1 ? 
ATOM   463  C  CG1 . VAL   A 1 63  ? -12.787 38.723 50.757 1.000 23.923  ? 62  VAL   AAA CG1 1 ? 
ATOM   464  C  CG2 . VAL   A 1 63  ? -11.697 36.982 49.354 1.000 21.847  ? 62  VAL   AAA CG2 1 ? 
ATOM   465  N  N   . GLY   A 1 64  ? -9.169  35.706 52.265 1.000 21.803  ? 63  GLY   AAA N   1 ? 
ATOM   466  C  CA  . GLY   A 1 64  ? -8.627  34.374 52.650 1.000 21.115  ? 63  GLY   AAA CA  1 ? 
ATOM   467  C  C   . GLY   A 1 64  ? -8.173  33.519 51.474 1.000 20.705  ? 63  GLY   AAA C   1 ? 
ATOM   468  O  O   . GLY   A 1 64  ? -6.983  33.142 51.441 1.000 27.617  ? 63  GLY   AAA O   1 ? 
ATOM   469  N  N   . HIS   A 1 65  ? -9.061  33.276 50.502 1.000 21.837  ? 64  HIS   AAA N   1 ? 
ATOM   470  C  CA  . HIS   A 1 65  ? -8.794  32.488 49.267 1.000 24.544  ? 64  HIS   AAA CA  1 ? 
ATOM   471  C  C   . HIS   A 1 65  ? -8.337  33.386 48.114 1.000 21.838  ? 64  HIS   AAA C   1 ? 
ATOM   472  O  O   . HIS   A 1 65  ? -7.829  32.880 47.084 1.000 22.180  ? 64  HIS   AAA O   1 ? 
ATOM   473  C  CB  . HIS   A 1 65  ? -10.056 31.717 48.942 1.000 23.574  ? 64  HIS   AAA CB  1 ? 
ATOM   474  C  CG  . HIS   A 1 65  ? -11.198 32.566 48.513 1.000 21.769  ? 64  HIS   AAA CG  1 ? 
ATOM   475  N  ND1 . HIS   A 1 65  ? -12.205 32.960 49.383 1.000 25.997  ? 64  HIS   AAA ND1 1 ? 
ATOM   476  C  CD2 . HIS   A 1 65  ? -11.549 32.998 47.289 1.000 20.801  ? 64  HIS   AAA CD2 1 ? 
ATOM   477  C  CE1 . HIS   A 1 65  ? -13.103 33.666 48.712 1.000 24.418  ? 64  HIS   AAA CE1 1 ? 
ATOM   478  N  NE2 . HIS   A 1 65  ? -12.753 33.678 47.427 1.000 26.900  ? 64  HIS   AAA NE2 1 ? 
ATOM   479  N  N   . SER   A 1 66  ? -8.555  34.708 48.283 1.000 20.976  ? 65  SER   AAA N   1 ? 
ATOM   480  C  CA  . SER   A 1 66  ? -8.357  35.694 47.206 1.000 19.518  ? 65  SER   AAA CA  1 ? 
ATOM   481  C  C   . SER   A 1 66  ? -8.322  37.101 47.817 1.000 18.710  ? 65  SER   AAA C   1 ? 
ATOM   482  O  O   . SER   A 1 66  ? -8.328  37.261 49.070 1.000 19.359  ? 65  SER   AAA O   1 ? 
ATOM   483  C  CB  . SER   A 1 66  ? -9.449  35.566 46.160 1.000 22.521  ? 65  SER   AAA CB  1 ? 
ATOM   484  O  OG  . SER   A 1 66  ? -9.074  36.204 44.935 1.000 22.912  ? 65  SER   AAA OG  1 ? 
ATOM   485  N  N   . PHE   A 1 67  ? -8.310  38.103 46.953 1.000 20.020  ? 66  PHE   AAA N   1 ? 
ATOM   486  C  CA  . PHE   A 1 67  ? -8.575  39.495 47.395 1.000 17.311  ? 66  PHE   AAA CA  1 ? 
ATOM   487  C  C   . PHE   A 1 67  ? -9.599  40.053 46.422 1.000 17.083  ? 66  PHE   AAA C   1 ? 
ATOM   488  O  O   . PHE   A 1 67  ? -9.614  39.713 45.219 1.000 18.729  ? 66  PHE   AAA O   1 ? 
ATOM   489  C  CB  . PHE   A 1 67  ? -7.298  40.330 47.487 1.000 17.955  ? 66  PHE   AAA CB  1 ? 
ATOM   490  C  CG  . PHE   A 1 67  ? -6.655  40.660 46.175 1.000 18.438  ? 66  PHE   AAA CG  1 ? 
ATOM   491  C  CD1 . PHE   A 1 67  ? -5.711  39.844 45.595 1.000 21.513  ? 66  PHE   AAA CD1 1 ? 
ATOM   492  C  CD2 . PHE   A 1 67  ? -6.993  41.849 45.532 1.000 19.683  ? 66  PHE   AAA CD2 1 ? 
ATOM   493  C  CE1 . PHE   A 1 67  ? -5.127  40.182 44.388 1.000 20.164  ? 66  PHE   AAA CE1 1 ? 
ATOM   494  C  CE2 . PHE   A 1 67  ? -6.433  42.165 44.311 1.000 20.101  ? 66  PHE   AAA CE2 1 ? 
ATOM   495  C  CZ  . PHE   A 1 67  ? -5.458  41.364 43.768 1.000 21.056  ? 66  PHE   AAA CZ  1 ? 
ATOM   496  N  N   . HIS   A 1 68  ? -10.419 40.951 46.940 1.000 18.386  ? 67  HIS   AAA N   1 ? 
ATOM   497  C  CA  . HIS   A 1 68  ? -11.474 41.591 46.147 1.000 18.610  ? 67  HIS   AAA CA  1 ? 
ATOM   498  C  C   . HIS   A 1 68  ? -11.301 43.116 46.158 1.000 18.943  ? 67  HIS   AAA C   1 ? 
ATOM   499  O  O   . HIS   A 1 68  ? -10.957 43.659 47.208 1.000 19.159  ? 67  HIS   AAA O   1 ? 
ATOM   500  C  CB  . HIS   A 1 68  ? -12.832 41.242 46.728 1.000 20.855  ? 67  HIS   AAA CB  1 ? 
ATOM   501  C  CG  . HIS   A 1 68  ? -13.186 39.791 46.615 1.000 21.908  ? 67  HIS   AAA CG  1 ? 
ATOM   502  N  ND1 . HIS   A 1 68  ? -14.268 39.291 47.300 1.000 22.649  ? 67  HIS   AAA ND1 1 ? 
ATOM   503  C  CD2 . HIS   A 1 68  ? -12.707 38.817 45.818 1.000 19.708  ? 67  HIS   AAA CD2 1 ? 
ATOM   504  C  CE1 . HIS   A 1 68  ? -14.417 38.005 46.983 1.000 24.397  ? 67  HIS   AAA CE1 1 ? 
ATOM   505  N  NE2 . HIS   A 1 68  ? -13.496 37.709 46.036 1.000 23.701  ? 67  HIS   AAA NE2 1 ? 
ATOM   506  N  N   . VAL   A 1 69  ? -11.585 43.680 45.013 1.000 18.412  ? 68  VAL   AAA N   1 ? 
ATOM   507  C  CA  . VAL   A 1 69  ? -11.769 45.169 44.988 1.000 19.320  ? 68  VAL   AAA CA  1 ? 
ATOM   508  C  C   . VAL   A 1 69  ? -13.256 45.425 44.762 1.000 18.296  ? 68  VAL   AAA C   1 ? 
ATOM   509  O  O   . VAL   A 1 69  ? -13.760 45.158 43.636 1.000 19.842  ? 68  VAL   AAA O   1 ? 
ATOM   510  C  CB  . VAL   A 1 69  ? -10.886 45.772 43.904 1.000 19.707  ? 68  VAL   AAA CB  1 ? 
ATOM   511  C  CG1 . VAL   A 1 69  ? -11.080 47.305 43.843 1.000 20.632  ? 68  VAL   AAA CG1 1 ? 
ATOM   512  C  CG2 . VAL   A 1 69  ? -9.434  45.452 44.167 1.000 21.519  ? 68  VAL   AAA CG2 1 ? 
ATOM   513  N  N   . ASN   A 1 70  ? -13.895 46.053 45.746 1.000 19.021  ? 69  ASN   AAA N   1 ? 
ATOM   514  C  CA  . ASN   A 1 70  ? -15.351 46.319 45.740 1.000 18.929  ? 69  ASN   AAA CA  1 ? 
ATOM   515  C  C   . ASN   A 1 70  ? -15.624 47.770 45.310 1.000 19.219  ? 69  ASN   AAA C   1 ? 
ATOM   516  O  O   . ASN   A 1 70  ? -14.762 48.695 45.595 1.000 19.153  ? 69  ASN   AAA O   1 ? 
ATOM   517  C  CB  . ASN   A 1 70  ? -15.940 46.021 47.119 1.000 20.625  ? 69  ASN   AAA CB  1 ? 
ATOM   518  C  CG  . ASN   A 1 70  ? -15.958 44.532 47.385 1.000 23.494  ? 69  ASN   AAA CG  1 ? 
ATOM   519  O  OD1 . ASN   A 1 70  ? -16.160 43.793 46.445 1.000 26.692  ? 69  ASN   AAA OD1 1 ? 
ATOM   520  N  ND2 . ASN   A 1 70  ? -15.683 44.108 48.600 1.000 38.280  ? 69  ASN   AAA ND2 1 ? 
ATOM   521  N  N   . PHE   A 1 71  ? -16.753 47.910 44.620 1.000 19.630  ? 70  PHE   AAA N   1 ? 
ATOM   522  C  CA  . PHE   A 1 71  ? -17.273 49.210 44.129 1.000 19.862  ? 70  PHE   AAA CA  1 ? 
ATOM   523  C  C   . PHE   A 1 71  ? -18.604 49.505 44.801 1.000 21.319  ? 70  PHE   AAA C   1 ? 
ATOM   524  O  O   . PHE   A 1 71  ? -19.460 48.668 45.046 1.000 23.585  ? 70  PHE   AAA O   1 ? 
ATOM   525  C  CB  . PHE   A 1 71  ? -17.376 49.211 42.596 1.000 21.199  ? 70  PHE   AAA CB  1 ? 
ATOM   526  C  CG  . PHE   A 1 71  ? -16.020 49.114 41.949 1.000 21.169  ? 70  PHE   AAA CG  1 ? 
ATOM   527  C  CD1 . PHE   A 1 71  ? -15.339 47.899 41.885 1.000 21.102  ? 70  PHE   AAA CD1 1 ? 
ATOM   528  C  CD2 . PHE   A 1 71  ? -15.433 50.231 41.378 1.000 19.554  ? 70  PHE   AAA CD2 1 ? 
ATOM   529  C  CE1 . PHE   A 1 71  ? -14.076 47.843 41.320 1.000 22.156  ? 70  PHE   AAA CE1 1 ? 
ATOM   530  C  CE2 . PHE   A 1 71  ? -14.166 50.181 40.841 1.000 20.900  ? 70  PHE   AAA CE2 1 ? 
ATOM   531  C  CZ  . PHE   A 1 71  ? -13.490 48.985 40.815 1.000 23.156  ? 70  PHE   AAA CZ  1 ? 
ATOM   532  N  N   . GLU   A 1 72  ? -18.815 50.796 44.997 1.000 21.119  ? 71  GLU   AAA N   1 ? 
ATOM   533  C  CA  . GLU   A 1 72  ? -20.127 51.343 45.388 1.000 21.935  ? 71  GLU   AAA CA  1 ? 
ATOM   534  C  C   . GLU   A 1 72  ? -21.080 50.971 44.264 1.000 21.099  ? 71  GLU   AAA C   1 ? 
ATOM   535  O  O   . GLU   A 1 72  ? -20.739 51.216 43.082 1.000 22.826  ? 71  GLU   AAA O   1 ? 
ATOM   536  C  CB  . GLU   A 1 72  ? -20.068 52.879 45.537 1.000 24.796  ? 71  GLU   AAA CB  1 ? 
ATOM   537  C  CG  . GLU   A 1 72  ? -19.183 53.381 46.679 1.000 31.081  ? 71  GLU   AAA CG  1 ? 
ATOM   538  C  CD  . GLU   A 1 72  ? -19.093 54.902 46.833 1.000 34.612  ? 71  GLU   AAA CD  1 ? 
ATOM   539  O  OE1 . GLU   A 1 72  ? -19.799 55.595 46.061 1.000 35.405  ? 71  GLU   AAA OE1 1 ? 
ATOM   540  O  OE2 . GLU   A 1 72  ? -18.292 55.366 47.686 1.000 34.707  ? 71  GLU   AAA OE2 1 ? 
ATOM   541  N  N   . ASP   A 1 73  ? -22.226 50.410 44.599 1.000 22.895  ? 72  ASP   AAA N   1 ? 
ATOM   542  C  CA  . ASP   A 1 73  ? -23.196 50.004 43.558 1.000 24.214  ? 72  ASP   AAA CA  1 ? 
ATOM   543  C  C   . ASP   A 1 73  ? -24.611 50.495 43.877 1.000 28.111  ? 72  ASP   AAA C   1 ? 
ATOM   544  O  O   . ASP   A 1 73  ? -25.574 49.747 43.582 1.000 27.737  ? 72  ASP   AAA O   1 ? 
ATOM   545  C  CB  . ASP   A 1 73  ? -23.156 48.488 43.425 1.000 24.963  ? 72  ASP   AAA CB  1 ? 
ATOM   546  C  CG  . ASP   A 1 73  ? -23.609 47.737 44.664 1.000 28.409  ? 72  ASP   AAA CG  1 ? 
ATOM   547  O  OD1 . ASP   A 1 73  ? -23.637 48.345 45.745 1.000 28.246  ? 72  ASP   AAA OD1 1 ? 
ATOM   548  O  OD2 . ASP   A 1 73  ? -23.933 46.519 44.507 1.000 26.100  ? 72  ASP   AAA OD2 1 ? 
ATOM   549  N  N   . ASN   A 1 74  ? -24.731 51.734 44.354 1.000 24.914  ? 73  ASN   AAA N   1 ? 
ATOM   550  C  CA  . ASN   A 1 74  ? -26.023 52.346 44.753 1.000 29.140  ? 73  ASN   AAA CA  1 ? 
ATOM   551  C  C   . ASN   A 1 74  ? -26.691 52.963 43.519 1.000 27.515  ? 73  ASN   AAA C   1 ? 
ATOM   552  O  O   . ASN   A 1 74  ? -27.897 53.331 43.588 1.000 36.558  ? 73  ASN   AAA O   1 ? 
ATOM   553  C  CB  . ASN   A 1 74  ? -25.796 53.321 45.908 1.000 30.820  ? 73  ASN   AAA CB  1 ? 
ATOM   554  C  CG  . ASN   A 1 74  ? -24.766 54.389 45.595 1.000 36.857  ? 73  ASN   AAA CG  1 ? 
ATOM   555  O  OD1 . ASN   A 1 74  ? -25.115 55.556 45.349 1.000 47.123  ? 73  ASN   AAA OD1 1 ? 
ATOM   556  N  ND2 . ASN   A 1 74  ? -23.487 54.024 45.665 1.000 29.809  ? 73  ASN   AAA ND2 1 ? 
ATOM   557  N  N   . ASP   A 1 75  ? -25.972 53.113 42.416 1.000 30.601  ? 74  ASP   AAA N   1 ? 
ATOM   558  C  CA  . ASP   A 1 75  ? -26.545 53.762 41.210 1.000 33.779  ? 74  ASP   AAA CA  1 ? 
ATOM   559  C  C   . ASP   A 1 75  ? -25.791 53.290 39.970 1.000 30.541  ? 74  ASP   AAA C   1 ? 
ATOM   560  O  O   . ASP   A 1 75  ? -24.895 52.428 40.112 1.000 29.401  ? 74  ASP   AAA O   1 ? 
ATOM   561  C  CB  . ASP   A 1 75  ? -26.555 55.300 41.376 1.000 33.314  ? 74  ASP   AAA CB  1 ? 
ATOM   562  C  CG  . ASP   A 1 75  ? -25.180 55.970 41.471 1.000 37.205  ? 74  ASP   AAA CG  1 ? 
ATOM   563  O  OD1 . ASP   A 1 75  ? -24.133 55.296 41.182 1.000 34.546  ? 74  ASP   AAA OD1 1 ? 
ATOM   564  O  OD2 . ASP   A 1 75  ? -25.153 57.229 41.777 1.000 39.002  ? 74  ASP   AAA OD2 1 ? 
ATOM   565  N  N   . ASN   A 1 76  ? -26.132 53.868 38.817 1.000 30.077  ? 75  ASN   AAA N   1 ? 
ATOM   566  C  CA  . ASN   A 1 76  ? -25.601 53.466 37.494 1.000 30.027  ? 75  ASN   AAA CA  1 ? 
ATOM   567  C  C   . ASN   A 1 76  ? -24.407 54.311 37.059 1.000 26.118  ? 75  ASN   AAA C   1 ? 
ATOM   568  O  O   . ASN   A 1 76  ? -24.217 54.431 35.849 1.000 31.211  ? 75  ASN   AAA O   1 ? 
ATOM   569  C  CB  . ASN   A 1 76  ? -26.691 53.421 36.430 1.000 33.455  ? 75  ASN   AAA CB  1 ? 
ATOM   570  C  CG  . ASN   A 1 76  ? -27.573 52.200 36.594 1.000 35.848  ? 75  ASN   AAA CG  1 ? 
ATOM   571  O  OD1 . ASN   A 1 76  ? -27.141 51.150 37.120 1.000 31.679  ? 75  ASN   AAA OD1 1 ? 
ATOM   572  N  ND2 . ASN   A 1 76  ? -28.809 52.335 36.131 1.000 47.361  ? 75  ASN   AAA ND2 1 ? 
ATOM   573  N  N   . ARG   A 1 77  ? -23.559 54.733 38.000 1.000 27.549  ? 76  ARG   AAA N   1 ? 
ATOM   574  C  CA  . ARG   A 1 77  ? -22.266 55.396 37.675 1.000 25.351  ? 76  ARG   AAA CA  1 ? 
ATOM   575  C  C   . ARG   A 1 77  ? -21.340 54.464 36.879 1.000 27.465  ? 76  ARG   AAA C   1 ? 
ATOM   576  O  O   . ARG   A 1 77  ? -20.628 54.967 35.964 1.000 29.741  ? 76  ARG   AAA O   1 ? 
ATOM   577  C  CB  . ARG   A 1 77  ? -21.609 55.910 38.956 1.000 27.023  ? 76  ARG   AAA CB  1 ? 
ATOM   578  C  CG  . ARG   A 1 77  ? -22.116 57.290 39.351 1.000 30.569  ? 76  ARG   AAA CG  1 ? 
ATOM   579  C  CD  . ARG   A 1 77  ? -21.629 57.773 40.698 1.000 28.959  ? 76  ARG   AAA CD  1 ? 
ATOM   580  N  NE  . ARG   A 1 77  ? -21.820 56.777 41.752 1.000 25.282  ? 76  ARG   AAA NE  1 ? 
ATOM   581  C  CZ  . ARG   A 1 77  ? -21.080 56.724 42.853 1.000 28.778  ? 76  ARG   AAA CZ  1 ? 
ATOM   582  N  NH1 . ARG   A 1 77  ? -20.094 57.614 43.029 1.000 27.830  ? 76  ARG   AAA NH1 1 ? 
ATOM   583  N  NH2 . ARG   A 1 77  ? -21.302 55.779 43.762 1.000 29.134  ? 76  ARG   AAA NH2 1 ? 
ATOM   584  N  N   . SER   A 1 78  ? -21.400 53.138 37.100 1.000 24.599  ? 77  SER   AAA N   1 ? 
ATOM   585  C  CA  . SER   A 1 78  ? -20.395 52.221 36.525 1.000 22.324  ? 77  SER   AAA CA  1 ? 
ATOM   586  C  C   . SER   A 1 78  ? -21.167 51.034 35.965 1.000 22.047  ? 77  SER   AAA C   1 ? 
ATOM   587  O  O   . SER   A 1 78  ? -21.736 50.261 36.766 1.000 24.968  ? 77  SER   AAA O   1 ? 
ATOM   588  C  CB  . SER   A 1 78  ? -19.396 51.820 37.540 1.000 20.281  ? 77  SER   AAA CB  1 ? 
ATOM   589  O  OG  . SER   A 1 78  ? -18.596 52.908 37.959 1.000 24.039  ? 77  SER   AAA OG  1 ? 
ATOM   590  N  N   . VAL   A 1 79  ? -21.276 50.976 34.645 1.000 22.460  ? 78  VAL   AAA N   1 ? 
ATOM   591  C  CA  . VAL   A 1 79  ? -22.177 49.993 33.998 1.000 23.176  ? 78  VAL   AAA CA  1 ? 
ATOM   592  C  C   . VAL   A 1 79  ? -21.479 49.290 32.839 1.000 25.227  ? 78  VAL   AAA C   1 ? 
ATOM   593  O  O   . VAL   A 1 79  ? -20.566 49.863 32.226 1.000 24.640  ? 78  VAL   AAA O   1 ? 
ATOM   594  C  CB  . VAL   A 1 79  ? -23.474 50.665 33.531 1.000 26.337  ? 78  VAL   AAA CB  1 ? 
ATOM   595  C  CG1 . VAL   A 1 79  ? -24.259 51.197 34.712 1.000 27.968  ? 78  VAL   AAA CG1 1 ? 
ATOM   596  C  CG2 . VAL   A 1 79  ? -23.187 51.762 32.528 1.000 30.835  ? 78  VAL   AAA CG2 1 ? 
ATOM   597  N  N   . LEU   A 1 80  ? -21.943 48.062 32.591 1.000 26.074  ? 79  LEU   AAA N   1 ? 
ATOM   598  C  CA  . LEU   A 1 80  ? -21.691 47.270 31.370 1.000 23.861  ? 79  LEU   AAA CA  1 ? 
ATOM   599  C  C   . LEU   A 1 80  ? -23.000 47.206 30.552 1.000 23.907  ? 79  LEU   AAA C   1 ? 
ATOM   600  O  O   . LEU   A 1 80  ? -24.078 46.970 31.158 1.000 26.200  ? 79  LEU   AAA O   1 ? 
ATOM   601  C  CB  . LEU   A 1 80  ? -21.240 45.889 31.837 1.000 22.482  ? 79  LEU   AAA CB  1 ? 
ATOM   602  C  CG  . LEU   A 1 80  ? -21.245 44.783 30.785 1.000 27.021  ? 79  LEU   AAA CG  1 ? 
ATOM   603  C  CD1 . LEU   A 1 80  ? -20.320 45.144 29.640 1.000 29.050  ? 79  LEU   AAA CD1 1 ? 
ATOM   604  C  CD2 . LEU   A 1 80  ? -20.818 43.478 31.417 1.000 27.492  ? 79  LEU   AAA CD2 1 ? 
ATOM   605  N  N   . LYS   A 1 81  ? -22.894 47.376 29.235 1.000 26.024  ? 80  LYS   AAA N   1 ? 
ATOM   606  C  CA  . LYS   A 1 81  ? -24.037 47.224 28.284 1.000 32.889  ? 80  LYS   AAA CA  1 ? 
ATOM   607  C  C   . LYS   A 1 81  ? -23.518 46.579 27.002 1.000 25.708  ? 80  LYS   AAA C   1 ? 
ATOM   608  O  O   . LYS   A 1 81  ? -22.272 46.395 26.876 1.000 29.095  ? 80  LYS   AAA O   1 ? 
ATOM   609  C  CB  . LYS   A 1 81  ? -24.648 48.584 27.908 1.000 38.776  ? 80  LYS   AAA CB  1 ? 
ATOM   610  C  CG  . LYS   A 1 81  ? -25.267 49.386 29.044 1.000 50.684  ? 80  LYS   AAA CG  1 ? 
ATOM   611  C  CD  . LYS   A 1 81  ? -25.644 50.828 28.678 1.000 65.840  ? 80  LYS   AAA CD  1 ? 
ATOM   612  C  CE  . LYS   A 1 81  ? -24.745 51.467 27.633 1.000 74.776  ? 80  LYS   AAA CE  1 ? 
ATOM   613  N  NZ  . LYS   A 1 81  ? -24.962 52.930 27.536 1.000 83.230  ? 80  LYS   AAA NZ  1 ? 
ATOM   614  N  N   . GLY   A 1 82  ? -24.445 46.277 26.090 1.000 29.561  ? 81  GLY   AAA N   1 ? 
ATOM   615  C  CA  . GLY   A 1 82  ? -24.148 45.675 24.779 1.000 28.332  ? 81  GLY   AAA CA  1 ? 
ATOM   616  C  C   . GLY   A 1 82  ? -23.866 44.178 24.886 1.000 25.489  ? 81  GLY   AAA C   1 ? 
ATOM   617  O  O   . GLY   A 1 82  ? -24.402 43.528 25.814 1.000 25.748  ? 81  GLY   AAA O   1 ? 
ATOM   618  N  N   . GLY   A 1 83  ? -23.021 43.660 24.000 1.000 26.605  ? 82  GLY   AAA N   1 ? 
ATOM   619  C  CA  . GLY   A 1 83  ? -22.724 42.210 23.912 1.000 28.588  ? 82  GLY   AAA CA  1 ? 
ATOM   620  C  C   . GLY   A 1 83  ? -24.043 41.471 23.745 1.000 30.405  ? 82  GLY   AAA C   1 ? 
ATOM   621  O  O   . GLY   A 1 83  ? -24.847 41.856 22.893 1.000 33.054  ? 82  GLY   AAA O   1 ? 
ATOM   622  N  N   . PRO   A 1 84  ? -24.343 40.444 24.575 1.000 27.405  ? 83  PRO   AAA N   1 ? 
ATOM   623  C  CA  . PRO   A 1 84  ? -25.610 39.725 24.468 1.000 30.160  ? 83  PRO   AAA CA  1 ? 
ATOM   624  C  C   . PRO   A 1 84  ? -26.784 40.349 25.235 1.000 30.816  ? 83  PRO   AAA C   1 ? 
ATOM   625  O  O   . PRO   A 1 84  ? -27.860 39.809 25.160 1.000 34.805  ? 83  PRO   AAA O   1 ? 
ATOM   626  C  CB  . PRO   A 1 84  ? -25.274 38.358 25.067 1.000 30.258  ? 83  PRO   AAA CB  1 ? 
ATOM   627  C  CG  . PRO   A 1 84  ? -24.211 38.622 26.091 1.000 31.110  ? 83  PRO   AAA CG  1 ? 
ATOM   628  C  CD  . PRO   A 1 84  ? -23.468 39.860 25.595 1.000 29.277  ? 83  PRO   AAA CD  1 ? 
ATOM   629  N  N   . PHE   A 1 85  ? -26.553 41.465 25.933 1.000 29.307  ? 84  PHE   AAA N   1 ? 
ATOM   630  C  CA  . PHE   A 1 85  ? -27.466 42.049 26.946 1.000 32.111  ? 84  PHE   AAA CA  1 ? 
ATOM   631  C  C   . PHE   A 1 85  ? -28.403 43.102 26.351 1.000 31.904  ? 84  PHE   AAA C   1 ? 
ATOM   632  O  O   . PHE   A 1 85  ? -27.980 43.927 25.512 1.000 33.160  ? 84  PHE   AAA O   1 ? 
ATOM   633  C  CB  . PHE   A 1 85  ? -26.642 42.709 28.046 1.000 29.772  ? 84  PHE   AAA CB  1 ? 
ATOM   634  C  CG  . PHE   A 1 85  ? -25.681 41.742 28.667 1.000 31.681  ? 84  PHE   AAA CG  1 ? 
ATOM   635  C  CD1 . PHE   A 1 85  ? -26.152 40.590 29.276 1.000 29.386  ? 84  PHE   AAA CD1 1 ? 
ATOM   636  C  CD2 . PHE   A 1 85  ? -24.321 41.977 28.635 1.000 31.702  ? 84  PHE   AAA CD2 1 ? 
ATOM   637  C  CE1 . PHE   A 1 85  ? -25.266 39.687 29.844 1.000 30.908  ? 84  PHE   AAA CE1 1 ? 
ATOM   638  C  CE2 . PHE   A 1 85  ? -23.440 41.090 29.221 1.000 28.294  ? 84  PHE   AAA CE2 1 ? 
ATOM   639  C  CZ  . PHE   A 1 85  ? -23.912 39.942 29.825 1.000 29.902  ? 84  PHE   AAA CZ  1 ? 
ATOM   640  N  N   . SER   A 1 86  ? -29.653 43.062 26.807 1.000 35.967  ? 85  SER   AAA N   1 ? 
ATOM   641  C  CA  . SER   A 1 86  ? -30.675 44.113 26.615 1.000 34.514  ? 85  SER   AAA CA  1 ? 
ATOM   642  C  C   . SER   A 1 86  ? -30.600 45.058 27.813 1.000 32.178  ? 85  SER   AAA C   1 ? 
ATOM   643  O  O   . SER   A 1 86  ? -30.879 46.252 27.665 1.000 43.592  ? 85  SER   AAA O   1 ? 
ATOM   644  C  CB  . SER   A 1 86  ? -32.040 43.515 26.509 1.000 45.007  ? 85  SER   AAA CB  1 ? 
ATOM   645  O  OG  . SER   A 1 86  ? -32.087 42.571 25.452 1.000 58.226  ? 85  SER   AAA OG  1 ? 
ATOM   646  N  N   . ASP   A 1 87  ? -30.250 44.497 28.965 1.000 33.985  ? 86  ASP   AAA N   1 ? 
ATOM   647  C  CA  . ASP   A 1 87  ? -30.237 45.194 30.273 1.000 39.254  ? 86  ASP   AAA CA  1 ? 
ATOM   648  C  C   . ASP   A 1 87  ? -28.872 45.848 30.493 1.000 31.591  ? 86  ASP   AAA C   1 ? 
ATOM   649  O  O   . ASP   A 1 87  ? -27.902 45.458 29.841 1.000 34.309  ? 86  ASP   AAA O   1 ? 
ATOM   650  C  CB  . ASP   A 1 87  ? -30.597 44.204 31.379 1.000 40.619  ? 86  ASP   AAA CB  1 ? 
ATOM   651  C  CG  . ASP   A 1 87  ? -32.017 43.661 31.270 1.000 38.316  ? 86  ASP   AAA CG  1 ? 
ATOM   652  O  OD1 . ASP   A 1 87  ? -32.934 44.394 30.764 1.000 42.835  ? 86  ASP   AAA OD1 1 ? 
ATOM   653  O  OD2 . ASP   A 1 87  ? -32.202 42.528 31.700 1.000 37.034  ? 86  ASP   AAA OD2 1 ? 
ATOM   654  N  N   . SER   A 1 88  ? -28.824 46.849 31.364 1.000 33.854  ? 87  SER   AAA N   1 ? 
ATOM   655  C  CA  . SER   A 1 88  ? -27.578 47.452 31.880 1.000 31.649  ? 87  SER   AAA CA  1 ? 
ATOM   656  C  C   . SER   A 1 88  ? -27.158 46.658 33.126 1.000 27.404  ? 87  SER   AAA C   1 ? 
ATOM   657  O  O   . SER   A 1 88  ? -28.013 46.338 33.955 1.000 28.361  ? 87  SER   AAA O   1 ? 
ATOM   658  C  CB  . SER   A 1 88  ? -27.766 48.947 32.148 1.000 35.379  ? 87  SER   AAA CB  1 ? 
ATOM   659  O  OG  . SER   A 1 88  ? -26.663 49.456 32.863 1.000 45.127  ? 87  SER   AAA OG  1 ? 
ATOM   660  N  N   . TYR   A 1 89  ? -25.878 46.341 33.256 1.000 24.672  ? 88  TYR   AAA N   1 ? 
ATOM   661  C  CA  . TYR   A 1 89  ? -25.342 45.667 34.454 1.000 23.196  ? 88  TYR   AAA CA  1 ? 
ATOM   662  C  C   . TYR   A 1 89  ? -24.409 46.600 35.220 1.000 21.098  ? 88  TYR   AAA C   1 ? 
ATOM   663  O  O   . TYR   A 1 89  ? -23.507 47.168 34.615 1.000 25.591  ? 88  TYR   AAA O   1 ? 
ATOM   664  C  CB  . TYR   A 1 89  ? -24.635 44.393 34.025 1.000 19.866  ? 88  TYR   AAA CB  1 ? 
ATOM   665  C  CG  . TYR   A 1 89  ? -25.581 43.293 33.590 1.000 23.369  ? 88  TYR   AAA CG  1 ? 
ATOM   666  C  CD1 . TYR   A 1 89  ? -26.248 43.339 32.382 1.000 23.386  ? 88  TYR   AAA CD1 1 ? 
ATOM   667  C  CD2 . TYR   A 1 89  ? -25.801 42.199 34.398 1.000 21.296  ? 88  TYR   AAA CD2 1 ? 
ATOM   668  C  CE1 . TYR   A 1 89  ? -27.133 42.349 31.985 1.000 24.515  ? 88  TYR   AAA CE1 1 ? 
ATOM   669  C  CE2 . TYR   A 1 89  ? -26.657 41.179 34.004 1.000 23.609  ? 88  TYR   AAA CE2 1 ? 
ATOM   670  C  CZ  . TYR   A 1 89  ? -27.357 41.268 32.808 1.000 23.364  ? 88  TYR   AAA CZ  1 ? 
ATOM   671  O  OH  . TYR   A 1 89  ? -28.224 40.286 32.363 1.000 28.888  ? 88  TYR   AAA OH  1 ? 
ATOM   672  N  N   . ARG   A 1 90  ? -24.575 46.639 36.532 1.000 21.955  ? 89  ARG   AAA N   1 ? 
ATOM   673  C  CA  . ARG   A 1 90  ? -23.849 47.548 37.444 1.000 20.887  ? 89  ARG   AAA CA  1 ? 
ATOM   674  C  C   . ARG   A 1 90  ? -22.601 46.846 37.986 1.000 20.285  ? 89  ARG   AAA C   1 ? 
ATOM   675  O  O   . ARG   A 1 90  ? -22.715 45.785 38.604 1.000 20.626  ? 89  ARG   AAA O   1 ? 
ATOM   676  C  CB  . ARG   A 1 90  ? -24.803 47.944 38.565 1.000 22.131  ? 89  ARG   AAA CB  1 ? 
ATOM   677  C  CG  . ARG   A 1 90  ? -24.268 48.981 39.528 1.000 25.792  ? 89  ARG   AAA CG  1 ? 
ATOM   678  C  CD  . ARG   A 1 90  ? -25.356 49.442 40.496 1.000 30.400  ? 89  ARG   AAA CD  1 ? 
ATOM   679  N  NE  . ARG   A 1 90  ? -26.512 50.059 39.851 1.000 28.359  ? 89  ARG   AAA NE  1 ? 
ATOM   680  C  CZ  . ARG   A 1 90  ? -27.651 50.407 40.455 1.000 27.874  ? 89  ARG   AAA CZ  1 ? 
ATOM   681  N  NH1 . ARG   A 1 90  ? -27.827 50.234 41.759 1.000 27.402  ? 89  ARG   AAA NH1 1 ? 
ATOM   682  N  NH2 . ARG   A 1 90  ? -28.624 50.935 39.728 1.000 34.481  ? 89  ARG   AAA NH2 1 ? 
ATOM   683  N  N   . LEU   A 1 91  ? -21.445 47.472 37.807 1.000 20.968  ? 90  LEU   AAA N   1 ? 
ATOM   684  C  CA  . LEU   A 1 91  ? -20.162 47.015 38.372 1.000 19.497  ? 90  LEU   AAA CA  1 ? 
ATOM   685  C  C   . LEU   A 1 91  ? -20.274 46.879 39.882 1.000 19.406  ? 90  LEU   AAA C   1 ? 
ATOM   686  O  O   . LEU   A 1 91  ? -20.823 47.796 40.542 1.000 21.575  ? 90  LEU   AAA O   1 ? 
ATOM   687  C  CB  . LEU   A 1 91  ? -19.073 48.020 38.012 1.000 19.807  ? 90  LEU   AAA CB  1 ? 
ATOM   688  C  CG  . LEU   A 1 91  ? -17.698 47.809 38.631 1.000 18.965  ? 90  LEU   AAA CG  1 ? 
ATOM   689  C  CD1 . LEU   A 1 91  ? -17.101 46.487 38.125 1.000 21.786  ? 90  LEU   AAA CD1 1 ? 
ATOM   690  C  CD2 . LEU   A 1 91  ? -16.739 48.926 38.279 1.000 22.256  ? 90  LEU   AAA CD2 1 ? 
ATOM   691  N  N   . PHE   A 1 92  ? -19.778 45.749 40.435 1.000 18.165  ? 91  PHE   AAA N   1 ? 
ATOM   692  C  CA  . PHE   A 1 92  ? -19.644 45.647 41.907 1.000 18.797  ? 91  PHE   AAA CA  1 ? 
ATOM   693  C  C   . PHE   A 1 92  ? -18.246 45.249 42.367 1.000 17.259  ? 91  PHE   AAA C   1 ? 
ATOM   694  O  O   . PHE   A 1 92  ? -17.947 45.525 43.566 1.000 19.350  ? 91  PHE   AAA O   1 ? 
ATOM   695  C  CB  . PHE   A 1 92  ? -20.783 44.834 42.529 1.000 19.522  ? 91  PHE   AAA CB  1 ? 
ATOM   696  C  CG  . PHE   A 1 92  ? -20.799 43.349 42.278 1.000 18.365  ? 91  PHE   AAA CG  1 ? 
ATOM   697  C  CD1 . PHE   A 1 92  ? -21.375 42.823 41.136 1.000 17.783  ? 91  PHE   AAA CD1 1 ? 
ATOM   698  C  CD2 . PHE   A 1 92  ? -20.216 42.501 43.196 1.000 18.722  ? 91  PHE   AAA CD2 1 ? 
ATOM   699  C  CE1 . PHE   A 1 92  ? -21.443 41.446 40.957 1.000 18.778  ? 91  PHE   AAA CE1 1 ? 
ATOM   700  C  CE2 . PHE   A 1 92  ? -20.236 41.112 42.989 1.000 18.920  ? 91  PHE   AAA CE2 1 ? 
ATOM   701  C  CZ  . PHE   A 1 92  ? -20.856 40.594 41.876 1.000 21.439  ? 91  PHE   AAA CZ  1 ? 
ATOM   702  N  N   . GLN   A 1 93  ? -17.479 44.501 41.549 1.000 19.132  ? 92  GLN   AAA N   1 ? 
ATOM   703  C  CA  . GLN   A 1 93  ? -16.215 43.956 42.076 1.000 18.635  ? 92  GLN   AAA CA  1 ? 
ATOM   704  C  C   . GLN   A 1 93  ? -15.308 43.573 40.913 1.000 16.999  ? 92  GLN   AAA C   1 ? 
ATOM   705  O  O   . GLN   A 1 93  ? -15.839 43.215 39.829 1.000 18.056  ? 92  GLN   AAA O   1 ? 
ATOM   706  C  CB  . GLN   A 1 93  ? -16.534 42.675 42.866 1.000 20.323  ? 92  GLN   AAA CB  1 ? 
ATOM   707  C  CG  . GLN   A 1 93  ? -15.326 42.031 43.516 1.000 24.709  ? 92  GLN   AAA CG  1 ? 
ATOM   708  C  CD  . GLN   A 1 93  ? -15.775 40.837 44.307 1.000 23.491  ? 92  GLN   AAA CD  1 ? 
ATOM   709  O  OE1 . GLN   A 1 93  ? -16.396 40.979 45.367 1.000 30.580  ? 92  GLN   AAA OE1 1 ? 
ATOM   710  N  NE2 . GLN   A 1 93  ? -15.475 39.654 43.773 1.000 21.254  ? 92  GLN   AAA NE2 1 ? 
ATOM   711  N  N   . PHE   A 1 94  ? -13.999 43.590 41.157 1.000 16.545  ? 93  PHE   AAA N   1 ? 
ATOM   712  C  CA  . PHE   A 1 94  ? -13.077 42.810 40.324 1.000 17.073  ? 93  PHE   AAA CA  1 ? 
ATOM   713  C  C   . PHE   A 1 94  ? -12.093 42.102 41.232 1.000 16.506  ? 93  PHE   AAA C   1 ? 
ATOM   714  O  O   . PHE   A 1 94  ? -11.927 42.398 42.387 1.000 17.510  ? 93  PHE   AAA O   1 ? 
ATOM   715  C  CB  . PHE   A 1 94  ? -12.377 43.580 39.218 1.000 19.577  ? 93  PHE   AAA CB  1 ? 
ATOM   716  C  CG  . PHE   A 1 94  ? -11.286 44.498 39.698 1.000 17.593  ? 93  PHE   AAA CG  1 ? 
ATOM   717  C  CD1 . PHE   A 1 94  ? -9.994  44.012 39.866 1.000 20.399  ? 93  PHE   AAA CD1 1 ? 
ATOM   718  C  CD2 . PHE   A 1 94  ? -11.533 45.856 39.920 1.000 17.456  ? 93  PHE   AAA CD2 1 ? 
ATOM   719  C  CE1 . PHE   A 1 94  ? -8.974  44.845 40.292 1.000 17.608  ? 93  PHE   AAA CE1 1 ? 
ATOM   720  C  CE2 . PHE   A 1 94  ? -10.496 46.663 40.319 1.000 19.135  ? 93  PHE   AAA CE2 1 ? 
ATOM   721  C  CZ  . PHE   A 1 94  ? -9.230  46.187 40.506 1.000 19.098  ? 93  PHE   AAA CZ  1 ? 
ATOM   722  N  N   . HIS   A 1 95  ? -11.645 40.960 40.696 1.000 18.462  ? 94  HIS   AAA N   1 ? 
ATOM   723  C  CA  . HIS   A 1 95  ? -10.654 40.101 41.395 1.000 17.886  ? 94  HIS   AAA CA  1 ? 
ATOM   724  C  C   . HIS   A 1 95  ? -9.892  39.286 40.359 1.000 16.833  ? 94  HIS   AAA C   1 ? 
ATOM   725  O  O   . HIS   A 1 95  ? -10.213 39.362 39.128 1.000 20.302  ? 94  HIS   AAA O   1 ? 
ATOM   726  C  CB  . HIS   A 1 95  ? -11.366 39.232 42.448 1.000 16.937  ? 94  HIS   AAA CB  1 ? 
ATOM   727  C  CG  . HIS   A 1 95  ? -12.333 38.297 41.823 1.000 18.414  ? 94  HIS   AAA CG  1 ? 
ATOM   728  N  ND1 . HIS   A 1 95  ? -13.679 38.473 41.914 1.000 20.202  ? 94  HIS   AAA ND1 1 ? 
ATOM   729  C  CD2 . HIS   A 1 95  ? -12.136 37.124 41.157 1.000 17.556  ? 94  HIS   AAA CD2 1 ? 
ATOM   730  C  CE1 . HIS   A 1 95  ? -14.287 37.492 41.245 1.000 20.625  ? 94  HIS   AAA CE1 1 ? 
ATOM   731  N  NE2 . HIS   A 1 95  ? -13.349 36.704 40.735 1.000 22.228  ? 94  HIS   AAA NE2 1 ? 
ATOM   732  N  N   . PHE   A 1 96  ? -8.977  38.453 40.854 1.000 16.687  ? 95  PHE   AAA N   1 ? 
ATOM   733  C  CA  . PHE   A 1 96  ? -8.105  37.678 39.960 1.000 16.828  ? 95  PHE   AAA CA  1 ? 
ATOM   734  C  C   . PHE   A 1 96  ? -8.173  36.251 40.471 1.000 17.719  ? 95  PHE   AAA C   1 ? 
ATOM   735  O  O   . PHE   A 1 96  ? -8.519  36.054 41.661 1.000 18.174  ? 95  PHE   AAA O   1 ? 
ATOM   736  C  CB  . PHE   A 1 96  ? -6.646  38.114 39.944 1.000 19.232  ? 95  PHE   AAA CB  1 ? 
ATOM   737  C  CG  . PHE   A 1 96  ? -6.472  39.559 39.566 1.000 18.462  ? 95  PHE   AAA CG  1 ? 
ATOM   738  C  CD1 . PHE   A 1 96  ? -6.608  40.530 40.527 1.000 18.104  ? 95  PHE   AAA CD1 1 ? 
ATOM   739  C  CD2 . PHE   A 1 96  ? -6.246  39.934 38.258 1.000 17.862  ? 95  PHE   AAA CD2 1 ? 
ATOM   740  C  CE1 . PHE   A 1 96  ? -6.500  41.876 40.191 1.000 17.921  ? 95  PHE   AAA CE1 1 ? 
ATOM   741  C  CE2 . PHE   A 1 96  ? -6.110  41.273 37.909 1.000 17.350  ? 95  PHE   AAA CE2 1 ? 
ATOM   742  C  CZ  . PHE   A 1 96  ? -6.256  42.230 38.882 1.000 19.174  ? 95  PHE   AAA CZ  1 ? 
ATOM   743  N  N   . HIS   A 1 97  ? -7.792  35.350 39.584 1.000 18.392  ? 96  HIS   AAA N   1 ? 
ATOM   744  C  CA  . HIS   A 1 97  ? -7.389  33.982 39.961 1.000 17.734  ? 96  HIS   AAA CA  1 ? 
ATOM   745  C  C   . HIS   A 1 97  ? -5.987  33.753 39.431 1.000 17.729  ? 96  HIS   AAA C   1 ? 
ATOM   746  O  O   . HIS   A 1 97  ? -5.631  34.296 38.368 1.000 17.672  ? 96  HIS   AAA O   1 ? 
ATOM   747  C  CB  . HIS   A 1 97  ? -8.361  32.973 39.392 1.000 18.019  ? 96  HIS   AAA CB  1 ? 
ATOM   748  C  CG  . HIS   A 1 97  ? -9.780  33.126 39.784 1.000 16.588  ? 96  HIS   AAA CG  1 ? 
ATOM   749  N  ND1 . HIS   A 1 97  ? -10.365 32.353 40.783 1.000 17.322  ? 96  HIS   AAA ND1 1 ? 
ATOM   750  C  CD2 . HIS   A 1 97  ? -10.738 34.038 39.406 1.000 19.116  ? 96  HIS   AAA CD2 1 ? 
ATOM   751  C  CE1 . HIS   A 1 97  ? -11.613 32.773 40.961 1.000 16.954  ? 96  HIS   AAA CE1 1 ? 
ATOM   752  N  NE2 . HIS   A 1 97  ? -11.880 33.763 40.102 1.000 19.367  ? 96  HIS   AAA NE2 1 ? 
ATOM   753  N  N   . TRP   A 1 98  ? -5.252  32.853 40.084 1.000 18.799  ? 97  TRP   AAA N   1 ? 
ATOM   754  C  CA  . TRP   A 1 98  ? -3.887  32.545 39.666 1.000 19.588  ? 97  TRP   AAA CA  1 ? 
ATOM   755  C  C   . TRP   A 1 98  ? -3.602  31.091 40.065 1.000 20.040  ? 97  TRP   AAA C   1 ? 
ATOM   756  O  O   . TRP   A 1 98  ? -4.377  30.560 40.873 1.000 21.041  ? 97  TRP   AAA O   1 ? 
ATOM   757  C  CB  . TRP   A 1 98  ? -2.872  33.461 40.285 1.000 17.896  ? 97  TRP   AAA CB  1 ? 
ATOM   758  C  CG  . TRP   A 1 98  ? -2.951  33.540 41.768 1.000 18.497  ? 97  TRP   AAA CG  1 ? 
ATOM   759  C  CD1 . TRP   A 1 98  ? -2.198  32.824 42.643 1.000 20.836  ? 97  TRP   AAA CD1 1 ? 
ATOM   760  C  CD2 . TRP   A 1 98  ? -3.696  34.496 42.564 1.000 19.208  ? 97  TRP   AAA CD2 1 ? 
ATOM   761  N  NE1 . TRP   A 1 98  ? -2.531  33.150 43.926 1.000 19.374  ? 97  TRP   AAA NE1 1 ? 
ATOM   762  C  CE2 . TRP   A 1 98  ? -3.394  34.226 43.909 1.000 17.883  ? 97  TRP   AAA CE2 1 ? 
ATOM   763  C  CE3 . TRP   A 1 98  ? -4.565  35.558 42.269 1.000 19.278  ? 97  TRP   AAA CE3 1 ? 
ATOM   764  C  CZ2 . TRP   A 1 98  ? -3.954  34.944 44.963 1.000 18.858  ? 97  TRP   AAA CZ2 1 ? 
ATOM   765  C  CZ3 . TRP   A 1 98  ? -5.121  36.271 43.316 1.000 17.036  ? 97  TRP   AAA CZ3 1 ? 
ATOM   766  C  CH2 . TRP   A 1 98  ? -4.834  35.959 44.636 1.000 17.575  ? 97  TRP   AAA CH2 1 ? 
ATOM   767  N  N   . GLY   A 1 99  ? -2.424  30.640 39.690 1.000 20.771  ? 98  GLY   AAA N   1 ? 
ATOM   768  C  CA  . GLY   A 1 99  ? -2.009  29.231 39.878 1.000 22.469  ? 98  GLY   AAA CA  1 ? 
ATOM   769  C  C   . GLY   A 1 99  ? -0.742  29.149 40.702 1.000 28.091  ? 98  GLY   AAA C   1 ? 
ATOM   770  O  O   . GLY   A 1 99  ? -0.156  30.177 40.992 1.000 26.558  ? 98  GLY   AAA O   1 ? 
ATOM   771  N  N   . SER   A 1 100 ? -0.299  27.955 41.081 1.000 32.483  ? 99  SER   AAA N   1 ? 
ATOM   772  C  CA  . SER   A 1 100 ? 0.882   27.790 41.966 1.000 39.430  ? 99  SER   AAA CA  1 ? 
ATOM   773  C  C   . SER   A 1 100 ? 2.161   28.070 41.153 1.000 41.832  ? 99  SER   AAA C   1 ? 
ATOM   774  O  O   . SER   A 1 100 ? 3.190   28.465 41.764 1.000 40.739  ? 99  SER   AAA O   1 ? 
ATOM   775  C  CB  . SER   A 1 100 ? 0.862   26.451 42.643 1.000 42.853  ? 99  SER   AAA CB  1 ? 
ATOM   776  O  OG  . SER   A 1 100 ? 0.712   25.431 41.676 1.000 51.315  ? 99  SER   AAA OG  1 ? 
ATOM   777  N  N   . THR   A 1 101 ? 2.101   27.944 39.827 1.000 36.799  ? 100 THR   AAA N   1 ? 
ATOM   778  C  CA  . THR   A 1 101 ? 3.231   28.290 38.922 1.000 37.278  ? 100 THR   AAA CA  1 ? 
ATOM   779  C  C   . THR   A 1 101 ? 2.665   28.958 37.670 1.000 31.612  ? 100 THR   AAA C   1 ? 
ATOM   780  O  O   . THR   A 1 101 ? 1.438   28.883 37.459 1.000 32.250  ? 100 THR   AAA O   1 ? 
ATOM   781  C  CB  . THR   A 1 101 ? 4.084   27.083 38.491 1.000 39.692  ? 100 THR   AAA CB  1 ? 
ATOM   782  O  OG1 . THR   A 1 101 ? 3.353   26.359 37.490 1.000 41.450  ? 100 THR   AAA OG1 1 ? 
ATOM   783  C  CG2 . THR   A 1 101 ? 4.466   26.146 39.617 1.000 44.612  ? 100 THR   AAA CG2 1 ? 
ATOM   784  N  N   . ASN   A 1 102 ? 3.560   29.468 36.824 1.000 27.606  ? 101 ASN   AAA N   1 ? 
ATOM   785  C  CA  . ASN   A 1 102 ? 3.210   30.257 35.616 1.000 27.226  ? 101 ASN   AAA CA  1 ? 
ATOM   786  C  C   . ASN   A 1 102 ? 2.446   29.370 34.631 1.000 27.125  ? 101 ASN   AAA C   1 ? 
ATOM   787  O  O   . ASN   A 1 102 ? 1.732   29.908 33.775 1.000 24.256  ? 101 ASN   AAA O   1 ? 
ATOM   788  C  CB  . ASN   A 1 102 ? 4.461   30.858 34.973 1.000 28.582  ? 101 ASN   AAA CB  1 ? 
ATOM   789  C  CG  . ASN   A 1 102 ? 5.045   32.025 35.754 1.000 27.168  ? 101 ASN   AAA CG  1 ? 
ATOM   790  O  OD1 . ASN   A 1 102 ? 4.498   32.460 36.761 1.000 29.340  ? 101 ASN   AAA OD1 1 ? 
ATOM   791  N  ND2 . ASN   A 1 102 ? 6.157   32.556 35.280 1.000 26.515  ? 101 ASN   AAA ND2 1 ? 
ATOM   792  N  N   . GLU   A 1 103 ? 2.621   28.040 34.750 1.000 25.456  ? 102 GLU   AAA N   1 ? 
ATOM   793  C  CA  . GLU   A 1 103 ? 2.105   27.007 33.817 1.000 30.520  ? 102 GLU   AAA CA  1 ? 
ATOM   794  C  C   . GLU   A 1 103 ? 0.557   26.998 33.789 1.000 28.903  ? 102 GLU   AAA C   1 ? 
ATOM   795  O  O   . GLU   A 1 103 ? -0.013  26.631 32.725 1.000 32.716  ? 102 GLU   AAA O   1 ? 
ATOM   796  C  CB  . GLU   A 1 103 ? 2.813   25.704 34.241 1.000 37.812  ? 102 GLU   AAA CB  1 ? 
ATOM   797  C  CG  . GLU   A 1 103 ? 2.404   24.462 33.491 1.000 47.976  ? 102 GLU   AAA CG  1 ? 
ATOM   798  C  CD  . GLU   A 1 103 ? 1.385   23.549 34.183 1.000 57.125  ? 102 GLU   AAA CD  1 ? 
ATOM   799  O  OE1 . GLU   A 1 103 ? 1.119   23.765 35.398 1.000 54.377  ? 102 GLU   AAA OE1 1 ? 
ATOM   800  O  OE2 . GLU   A 1 103 ? 0.861   22.597 33.507 1.000 67.684  ? 102 GLU   AAA OE2 1 ? 
ATOM   801  N  N   . HIS   A 1 104 ? -0.129  27.370 34.879 1.000 25.847  ? 103 HIS   AAA N   1 ? 
ATOM   802  C  CA  A HIS   A 1 104 ? -1.593  27.272 35.035 0.500 28.147  ? 103 HIS   AAA CA  1 ? 
ATOM   803  C  CA  B HIS   A 1 104 ? -1.636  27.369 34.903 0.500 26.106  ? 103 HIS   AAA CA  1 ? 
ATOM   804  C  C   . HIS   A 1 104 ? -2.000  28.467 35.897 1.000 27.436  ? 103 HIS   AAA C   1 ? 
ATOM   805  O  O   . HIS   A 1 104 ? -1.086  29.235 36.390 1.000 28.443  ? 103 HIS   AAA O   1 ? 
ATOM   806  C  CB  A HIS   A 1 104 ? -1.907  25.881 35.623 0.500 31.632  ? 103 HIS   AAA CB  1 ? 
ATOM   807  C  CB  B HIS   A 1 104 ? -2.354  25.973 35.139 0.500 23.502  ? 103 HIS   AAA CB  1 ? 
ATOM   808  C  CG  A HIS   A 1 104 ? -1.389  25.754 37.014 0.500 33.755  ? 103 HIS   AAA CG  1 ? 
ATOM   809  C  CG  B HIS   A 1 104 ? -3.869  25.843 34.908 0.500 26.028  ? 103 HIS   AAA CG  1 ? 
ATOM   810  N  ND1 A HIS   A 1 104 ? -0.067  25.420 37.277 0.500 28.136  ? 103 HIS   AAA ND1 1 ? 
ATOM   811  N  ND1 B HIS   A 1 104 ? -4.758  26.931 34.588 0.500 18.911  ? 103 HIS   AAA ND1 1 ? 
ATOM   812  C  CD2 A HIS   A 1 104 ? -2.007  25.968 38.219 0.500 32.228  ? 103 HIS   AAA CD2 1 ? 
ATOM   813  C  CD2 B HIS   A 1 104 ? -4.694  24.745 35.009 0.500 25.701  ? 103 HIS   AAA CD2 1 ? 
ATOM   814  C  CE1 A HIS   A 1 104 ? 0.107   25.410 38.582 0.500 27.776  ? 103 HIS   AAA CE1 1 ? 
ATOM   815  C  CE1 B HIS   A 1 104 ? -5.989  26.478 34.456 0.500 23.952  ? 103 HIS   AAA CE1 1 ? 
ATOM   816  N  NE2 A HIS   A 1 104 ? -1.060  25.768 39.180 0.500 30.293  ? 103 HIS   AAA NE2 1 ? 
ATOM   817  N  NE2 B HIS   A 1 104 ? -6.003  25.137 34.720 0.500 25.459  ? 103 HIS   AAA NE2 1 ? 
ATOM   818  N  N   . GLY   A 1 105 ? -3.257  28.687 36.072 1.000 24.261  ? 104 GLY   AAA N   1 ? 
ATOM   819  C  CA  . GLY   A 1 105 ? -3.653  29.827 36.897 1.000 23.871  ? 104 GLY   AAA CA  1 ? 
ATOM   820  C  C   . GLY   A 1 105 ? -4.925  30.424 36.387 1.000 19.725  ? 104 GLY   AAA C   1 ? 
ATOM   821  O  O   . GLY   A 1 105 ? -5.694  30.881 37.252 1.000 22.267  ? 104 GLY   AAA O   1 ? 
ATOM   822  N  N   . SER   A 1 106 ? -5.131  30.449 35.072 1.000 18.195  ? 105 SER   AAA N   1 ? 
ATOM   823  C  CA  . SER   A 1 106 ? -6.442  30.878 34.516 1.000 21.110  ? 105 SER   AAA CA  1 ? 
ATOM   824  C  C   . SER   A 1 106 ? -7.537  29.866 34.890 1.000 19.857  ? 105 SER   AAA C   1 ? 
ATOM   825  O  O   . SER   A 1 106 ? -7.243  28.675 35.263 1.000 19.199  ? 105 SER   AAA O   1 ? 
ATOM   826  C  CB  . SER   A 1 106 ? -6.415  31.153 33.041 1.000 18.658  ? 105 SER   AAA CB  1 ? 
ATOM   827  O  OG  . SER   A 1 106 ? -6.231  29.958 32.287 1.000 19.750  ? 105 SER   AAA OG  1 ? 
ATOM   828  N  N   . GLU   A 1 107 ? -8.772  30.315 34.860 1.000 17.807  ? 106 GLU   AAA N   1 ? 
ATOM   829  C  CA  . GLU   A 1 107 ? -9.943  29.442 35.080 1.000 18.790  ? 106 GLU   AAA CA  1 ? 
ATOM   830  C  C   . GLU   A 1 107 ? -10.397 28.969 33.723 1.000 20.111  ? 106 GLU   AAA C   1 ? 
ATOM   831  O  O   . GLU   A 1 107 ? -10.385 27.741 33.461 1.000 21.020  ? 106 GLU   AAA O   1 ? 
ATOM   832  C  CB  . GLU   A 1 107 ? -11.005 30.196 35.861 1.000 17.553  ? 106 GLU   AAA CB  1 ? 
ATOM   833  C  CG  . GLU   A 1 107 ? -10.541 30.430 37.290 1.000 20.118  ? 106 GLU   AAA CG  1 ? 
ATOM   834  C  CD  . GLU   A 1 107 ? -11.621 30.449 38.334 1.000 18.089  ? 106 GLU   AAA CD  1 ? 
ATOM   835  O  OE1 . GLU   A 1 107 ? -11.510 29.704 39.305 1.000 19.680  ? 106 GLU   AAA OE1 1 ? 
ATOM   836  O  OE2 . GLU   A 1 107 ? -12.524 31.350 38.205 1.000 22.274  ? 106 GLU   AAA OE2 1 ? 
ATOM   837  N  N   . HIS   A 1 108 ? -10.784 29.882 32.852 1.000 18.783  ? 107 HIS   AAA N   1 ? 
ATOM   838  C  CA  . HIS   A 1 108 ? -11.096 29.539 31.441 1.000 18.382  ? 107 HIS   AAA CA  1 ? 
ATOM   839  C  C   . HIS   A 1 108 ? -9.808  29.078 30.758 1.000 18.725  ? 107 HIS   AAA C   1 ? 
ATOM   840  O  O   . HIS   A 1 108 ? -8.716  29.555 31.109 1.000 19.308  ? 107 HIS   AAA O   1 ? 
ATOM   841  C  CB  . HIS   A 1 108 ? -11.803 30.714 30.751 1.000 19.040  ? 107 HIS   AAA CB  1 ? 
ATOM   842  C  CG  . HIS   A 1 108 ? -13.163 30.909 31.305 1.000 19.446  ? 107 HIS   AAA CG  1 ? 
ATOM   843  N  ND1 . HIS   A 1 108 ? -13.405 31.692 32.402 1.000 18.843  ? 107 HIS   AAA ND1 1 ? 
ATOM   844  C  CD2 . HIS   A 1 108 ? -14.350 30.363 30.975 1.000 20.637  ? 107 HIS   AAA CD2 1 ? 
ATOM   845  C  CE1 . HIS   A 1 108 ? -14.680 31.647 32.710 1.000 21.228  ? 107 HIS   AAA CE1 1 ? 
ATOM   846  N  NE2 . HIS   A 1 108 ? -15.286 30.795 31.860 1.000 19.642  ? 107 HIS   AAA NE2 1 ? 
ATOM   847  N  N   . THR   A 1 109 ? -9.954  28.179 29.784 1.000 20.204  ? 108 THR   AAA N   1 ? 
ATOM   848  C  CA  . THR   A 1 109 ? -8.878  27.805 28.836 1.000 21.508  ? 108 THR   AAA CA  1 ? 
ATOM   849  C  C   . THR   A 1 109 ? -9.406  28.001 27.416 1.000 21.559  ? 108 THR   AAA C   1 ? 
ATOM   850  O  O   . THR   A 1 109 ? -10.637 28.017 27.224 1.000 22.010  ? 108 THR   AAA O   1 ? 
ATOM   851  C  CB  . THR   A 1 109 ? -8.373  26.384 29.125 1.000 20.837  ? 108 THR   AAA CB  1 ? 
ATOM   852  O  OG1 . THR   A 1 109 ? -9.449  25.439 28.967 1.000 25.091  ? 108 THR   AAA OG1 1 ? 
ATOM   853  C  CG2 . THR   A 1 109 ? -7.829  26.264 30.532 1.000 21.502  ? 108 THR   AAA CG2 1 ? 
ATOM   854  N  N   . VAL   A 1 110 ? -8.488  28.118 26.445 1.000 20.401  ? 109 VAL   AAA N   1 ? 
ATOM   855  C  CA  . VAL   A 1 110 ? -8.887  28.284 25.025 1.000 21.726  ? 109 VAL   AAA CA  1 ? 
ATOM   856  C  C   . VAL   A 1 110 ? -8.160  27.227 24.210 1.000 22.646  ? 109 VAL   AAA C   1 ? 
ATOM   857  O  O   . VAL   A 1 110 ? -6.920  27.249 24.155 1.000 22.818  ? 109 VAL   AAA O   1 ? 
ATOM   858  C  CB  . VAL   A 1 110 ? -8.655  29.735 24.529 1.000 21.818  ? 109 VAL   AAA CB  1 ? 
ATOM   859  C  CG1 . VAL   A 1 110 ? -9.071  29.883 23.074 1.000 23.729  ? 109 VAL   AAA CG1 1 ? 
ATOM   860  C  CG2 . VAL   A 1 110 ? -9.404  30.710 25.413 1.000 23.844  ? 109 VAL   AAA CG2 1 ? 
ATOM   861  N  N   . ASP   A 1 111 ? -8.916  26.301 23.631 1.000 24.330  ? 110 ASP   AAA N   1 ? 
ATOM   862  C  CA  . ASP   A 1 111 ? -8.314  25.159 22.878 1.000 26.491  ? 110 ASP   AAA CA  1 ? 
ATOM   863  C  C   . ASP   A 1 111 ? -7.334  24.368 23.779 1.000 23.755  ? 110 ASP   AAA C   1 ? 
ATOM   864  O  O   . ASP   A 1 111 ? -6.279  23.968 23.315 1.000 25.096  ? 110 ASP   AAA O   1 ? 
ATOM   865  C  CB  . ASP   A 1 111 ? -7.711  25.697 21.573 1.000 25.090  ? 110 ASP   AAA CB  1 ? 
ATOM   866  C  CG  . ASP   A 1 111 ? -8.775  26.142 20.576 1.000 26.233  ? 110 ASP   AAA CG  1 ? 
ATOM   867  O  OD1 . ASP   A 1 111 ? -9.801  25.464 20.488 1.000 27.376  ? 110 ASP   AAA OD1 1 ? 
ATOM   868  O  OD2 . ASP   A 1 111 ? -8.577  27.181 19.881 1.000 27.298  ? 110 ASP   AAA OD2 1 ? 
ATOM   869  N  N   . GLY   A 1 112 ? -7.689  24.218 25.051 1.000 23.415  ? 111 GLY   AAA N   1 ? 
ATOM   870  C  CA  . GLY   A 1 112 ? -6.926  23.541 26.105 1.000 24.066  ? 111 GLY   AAA CA  1 ? 
ATOM   871  C  C   . GLY   A 1 112 ? -5.727  24.306 26.600 1.000 24.537  ? 111 GLY   AAA C   1 ? 
ATOM   872  O  O   . GLY   A 1 112 ? -5.082  23.838 27.514 1.000 25.478  ? 111 GLY   AAA O   1 ? 
ATOM   873  N  N   . VAL   A 1 113 ? -5.511  25.548 26.157 1.000 22.811  ? 112 VAL   AAA N   1 ? 
ATOM   874  C  CA  . VAL   A 1 113 ? -4.307  26.266 26.635 1.000 23.107  ? 112 VAL   AAA CA  1 ? 
ATOM   875  C  C   . VAL   A 1 113 ? -4.666  26.954 27.955 1.000 22.058  ? 112 VAL   AAA C   1 ? 
ATOM   876  O  O   . VAL   A 1 113 ? -5.754  27.565 28.049 1.000 23.296  ? 112 VAL   AAA O   1 ? 
ATOM   877  C  CB  . VAL   A 1 113 ? -3.793  27.239 25.568 1.000 26.037  ? 112 VAL   AAA CB  1 ? 
ATOM   878  C  CG1 . VAL   A 1 113 ? -2.638  28.067 26.145 1.000 23.800  ? 112 VAL   AAA CG1 1 ? 
ATOM   879  C  CG2 . VAL   A 1 113 ? -3.436  26.494 24.266 1.000 24.960  ? 112 VAL   AAA CG2 1 ? 
ATOM   880  N  N   . LYS   A 1 114 ? -3.785  26.820 28.932 1.000 20.938  ? 113 LYS   AAA N   1 ? 
ATOM   881  C  CA  . LYS   A 1 114 ? -3.921  27.326 30.318 1.000 22.253  ? 113 LYS   AAA CA  1 ? 
ATOM   882  C  C   . LYS   A 1 114 ? -3.062  28.589 30.378 1.000 20.684  ? 113 LYS   AAA C   1 ? 
ATOM   883  O  O   . LYS   A 1 114 ? -1.913  28.574 29.920 1.000 23.866  ? 113 LYS   AAA O   1 ? 
ATOM   884  C  CB  . LYS   A 1 114 ? -3.483  26.254 31.321 1.000 26.150  ? 113 LYS   AAA CB  1 ? 
ATOM   885  C  CG  . LYS   A 1 114 ? -4.313  24.978 31.241 1.000 27.573  ? 113 LYS   AAA CG  1 ? 
ATOM   886  C  CD  . LYS   A 1 114 ? -3.873  23.833 32.122 1.000 37.500  ? 113 LYS   AAA CD  1 ? 
ATOM   887  C  CE  . LYS   A 1 114 ? -2.482  23.301 31.843 1.000 48.003  ? 113 LYS   AAA CE  1 ? 
ATOM   888  N  NZ  . LYS   A 1 114 ? -2.283  21.966 32.468 1.000 57.837  ? 113 LYS   AAA NZ  1 ? 
ATOM   889  N  N   . TYR   A 1 115 ? -3.659  29.701 30.789 1.000 19.145  ? 114 TYR   AAA N   1 ? 
ATOM   890  C  CA  . TYR   A 1 115 ? -2.865  30.924 31.048 1.000 20.159  ? 114 TYR   AAA CA  1 ? 
ATOM   891  C  C   . TYR   A 1 115 ? -2.458  31.003 32.511 1.000 21.406  ? 114 TYR   AAA C   1 ? 
ATOM   892  O  O   . TYR   A 1 115 ? -2.871  30.160 33.321 1.000 22.595  ? 114 TYR   AAA O   1 ? 
ATOM   893  C  CB  . TYR   A 1 115 ? -3.650  32.072 30.434 1.000 19.784  ? 114 TYR   AAA CB  1 ? 
ATOM   894  C  CG  . TYR   A 1 115 ? -3.673  31.974 28.933 1.000 20.092  ? 114 TYR   AAA CG  1 ? 
ATOM   895  C  CD1 . TYR   A 1 115 ? -2.610  32.433 28.175 1.000 23.360  ? 114 TYR   AAA CD1 1 ? 
ATOM   896  C  CD2 . TYR   A 1 115 ? -4.712  31.355 28.257 1.000 20.159  ? 114 TYR   AAA CD2 1 ? 
ATOM   897  C  CE1 . TYR   A 1 115 ? -2.584  32.307 26.802 1.000 25.803  ? 114 TYR   AAA CE1 1 ? 
ATOM   898  C  CE2 . TYR   A 1 115 ? -4.699  31.216 26.883 1.000 22.618  ? 114 TYR   AAA CE2 1 ? 
ATOM   899  C  CZ  . TYR   A 1 115 ? -3.630  31.687 26.139 1.000 22.074  ? 114 TYR   AAA CZ  1 ? 
ATOM   900  O  OH  . TYR   A 1 115 ? -3.622  31.586 24.773 1.000 25.517  ? 114 TYR   AAA OH  1 ? 
ATOM   901  N  N   . SER   A 1 116 ? -1.706  32.050 32.880 1.000 20.385  ? 115 SER   AAA N   1 ? 
ATOM   902  C  CA  . SER   A 1 116 ? -1.064  32.156 34.209 1.000 19.525  ? 115 SER   AAA CA  1 ? 
ATOM   903  C  C   . SER   A 1 116 ? -2.034  32.752 35.239 1.000 17.921  ? 115 SER   AAA C   1 ? 
ATOM   904  O  O   . SER   A 1 116 ? -1.819  32.586 36.434 1.000 19.556  ? 115 SER   AAA O   1 ? 
ATOM   905  C  CB  . SER   A 1 116 ? 0.150   32.983 34.143 1.000 20.602  ? 115 SER   AAA CB  1 ? 
ATOM   906  O  OG  . SER   A 1 116 ? 1.094   32.475 33.239 1.000 24.850  ? 115 SER   AAA OG  1 ? 
ATOM   907  N  N   . ALA   A 1 117 ? -3.030  33.512 34.786 1.000 17.368  ? 116 ALA   AAA N   1 ? 
ATOM   908  C  CA  . ALA   A 1 117 ? -4.015  34.117 35.699 1.000 17.047  ? 116 ALA   AAA CA  1 ? 
ATOM   909  C  C   . ALA   A 1 117 ? -5.237  34.576 34.908 1.000 15.622  ? 116 ALA   AAA C   1 ? 
ATOM   910  O  O   . ALA   A 1 117 ? -5.251  34.485 33.649 1.000 17.269  ? 116 ALA   AAA O   1 ? 
ATOM   911  C  CB  . ALA   A 1 117 ? -3.367  35.238 36.468 1.000 20.612  ? 116 ALA   AAA CB  1 ? 
ATOM   912  N  N   . GLU   A 1 118 ? -6.232  35.072 35.628 1.000 17.157  ? 117 GLU   AAA N   1 ? 
ATOM   913  C  CA  . GLU   A 1 118 ? -7.456  35.572 34.958 1.000 16.368  ? 117 GLU   AAA CA  1 ? 
ATOM   914  C  C   . GLU   A 1 118 ? -8.036  36.671 35.823 1.000 15.685  ? 117 GLU   AAA C   1 ? 
ATOM   915  O  O   . GLU   A 1 118 ? -8.043  36.545 37.056 1.000 19.083  ? 117 GLU   AAA O   1 ? 
ATOM   916  C  CB  . GLU   A 1 118 ? -8.413  34.393 34.774 1.000 17.270  ? 117 GLU   AAA CB  1 ? 
ATOM   917  C  CG  . GLU   A 1 118 ? -9.663  34.680 33.936 1.000 17.307  ? 117 GLU   AAA CG  1 ? 
ATOM   918  C  CD  . GLU   A 1 118 ? -10.473 33.460 33.546 1.000 17.378  ? 117 GLU   AAA CD  1 ? 
ATOM   919  O  OE1 . GLU   A 1 118 ? -11.701 33.552 33.471 1.000 19.056  ? 117 GLU   AAA OE1 1 ? 
ATOM   920  O  OE2 . GLU   A 1 118 ? -9.813  32.411 33.320 1.000 19.570  ? 117 GLU   AAA OE2 1 ? 
ATOM   921  N  N   . LEU   A 1 119 ? -8.485  37.726 35.137 1.000 16.792  ? 118 LEU   AAA N   1 ? 
ATOM   922  C  CA  . LEU   A 1 119 ? -9.193  38.878 35.755 1.000 17.422  ? 118 LEU   AAA CA  1 ? 
ATOM   923  C  C   . LEU   A 1 119 ? -10.689 38.691 35.529 1.000 17.679  ? 118 LEU   AAA C   1 ? 
ATOM   924  O  O   . LEU   A 1 119 ? -11.080 38.447 34.382 1.000 17.640  ? 118 LEU   AAA O   1 ? 
ATOM   925  C  CB  . LEU   A 1 119 ? -8.675  40.164 35.083 1.000 16.881  ? 118 LEU   AAA CB  1 ? 
ATOM   926  C  CG  . LEU   A 1 119 ? -9.554  41.403 35.252 1.000 17.510  ? 118 LEU   AAA CG  1 ? 
ATOM   927  C  CD1 . LEU   A 1 119 ? -9.522  41.906 36.702 1.000 17.840  ? 118 LEU   AAA CD1 1 ? 
ATOM   928  C  CD2 . LEU   A 1 119 ? -9.101  42.504 34.288 1.000 20.134  ? 118 LEU   AAA CD2 1 ? 
ATOM   929  N  N   . HIS   A 1 120 ? -11.468 38.818 36.590 1.000 20.589  ? 119 HIS   AAA N   1 ? 
ATOM   930  C  CA  . HIS   A 1 120 ? -12.947 38.821 36.595 1.000 20.215  ? 119 HIS   AAA CA  1 ? 
ATOM   931  C  C   . HIS   A 1 120 ? -13.389 40.260 36.966 1.000 19.699  ? 119 HIS   AAA C   1 ? 
ATOM   932  O  O   . HIS   A 1 120 ? -13.076 40.653 38.078 1.000 20.633  ? 119 HIS   AAA O   1 ? 
ATOM   933  C  CB  . HIS   A 1 120 ? -13.456 37.779 37.575 1.000 19.503  ? 119 HIS   AAA CB  1 ? 
ATOM   934  C  CG  . HIS   A 1 120 ? -13.159 36.413 37.039 1.000 18.773  ? 119 HIS   AAA CG  1 ? 
ATOM   935  N  ND1 . HIS   A 1 120 ? -13.217 35.218 37.840 1.000 22.047  ? 119 HIS   AAA ND1 1 ? 
ATOM   936  C  CD2 . HIS   A 1 120 ? -12.870 36.047 35.756 1.000 17.751  ? 119 HIS   AAA CD2 1 ? 
ATOM   937  C  CE1 . HIS   A 1 120 ? -12.931 34.224 37.022 1.000 16.226  ? 119 HIS   AAA CE1 1 ? 
ATOM   938  N  NE2 . HIS   A 1 120 ? -12.772 34.641 35.736 1.000 16.306  ? 119 HIS   AAA NE2 1 ? 
ATOM   939  N  N   . VAL   A 1 121 ? -14.275 40.800 36.151 1.000 19.556  ? 120 VAL   AAA N   1 ? 
ATOM   940  C  CA  . VAL   A 1 121 ? -14.952 42.103 36.453 1.000 18.742  ? 120 VAL   AAA CA  1 ? 
ATOM   941  C  C   . VAL   A 1 121 ? -16.449 41.739 36.525 1.000 16.690  ? 120 VAL   AAA C   1 ? 
ATOM   942  O  O   . VAL   A 1 121 ? -17.037 41.372 35.451 1.000 17.707  ? 120 VAL   AAA O   1 ? 
ATOM   943  C  CB  . VAL   A 1 121 ? -14.642 43.159 35.382 1.000 19.972  ? 120 VAL   AAA CB  1 ? 
ATOM   944  C  CG1 . VAL   A 1 121 ? -15.271 44.453 35.821 1.000 19.712  ? 120 VAL   AAA CG1 1 ? 
ATOM   945  C  CG2 . VAL   A 1 121 ? -13.150 43.352 35.125 1.000 17.643  ? 120 VAL   AAA CG2 1 ? 
ATOM   946  N  N   . ALA   A 1 122 ? -17.021 41.792 37.723 1.000 17.586  ? 121 ALA   AAA N   1 ? 
ATOM   947  C  CA  . ALA   A 1 122 ? -18.375 41.281 37.999 1.000 16.568  ? 121 ALA   AAA CA  1 ? 
ATOM   948  C  C   . ALA   A 1 122 ? -19.400 42.420 38.073 1.000 19.094  ? 121 ALA   AAA C   1 ? 
ATOM   949  O  O   . ALA   A 1 122 ? -19.098 43.495 38.684 1.000 18.731  ? 121 ALA   AAA O   1 ? 
ATOM   950  C  CB  . ALA   A 1 122 ? -18.389 40.468 39.273 1.000 19.471  ? 121 ALA   AAA CB  1 ? 
ATOM   951  N  N   . HIS   A 1 123 ? -20.596 42.148 37.581 1.000 17.253  ? 122 HIS   AAA N   1 ? 
ATOM   952  C  CA  . HIS   A 1 123 ? -21.704 43.126 37.484 1.000 17.746  ? 122 HIS   AAA CA  1 ? 
ATOM   953  C  C   . HIS   A 1 123 ? -23.011 42.427 37.837 1.000 19.723  ? 122 HIS   AAA C   1 ? 
ATOM   954  O  O   . HIS   A 1 123 ? -23.118 41.173 37.595 1.000 22.410  ? 122 HIS   AAA O   1 ? 
ATOM   955  C  CB  . HIS   A 1 123 ? -21.775 43.674 36.061 1.000 19.068  ? 122 HIS   AAA CB  1 ? 
ATOM   956  C  CG  . HIS   A 1 123 ? -20.483 44.091 35.450 1.000 17.592  ? 122 HIS   AAA CG  1 ? 
ATOM   957  N  ND1 . HIS   A 1 123 ? -19.522 43.195 34.996 1.000 21.192  ? 122 HIS   AAA ND1 1 ? 
ATOM   958  C  CD2 . HIS   A 1 123 ? -20.025 45.322 35.107 1.000 19.830  ? 122 HIS   AAA CD2 1 ? 
ATOM   959  C  CE1 . HIS   A 1 123 ? -18.499 43.849 34.460 1.000 18.328  ? 122 HIS   AAA CE1 1 ? 
ATOM   960  N  NE2 . HIS   A 1 123 ? -18.806 45.179 34.535 1.000 18.277  ? 122 HIS   AAA NE2 1 ? 
ATOM   961  N  N   . TRP   A 1 124 ? -24.018 43.169 38.253 1.000 20.637  ? 123 TRP   AAA N   1 ? 
ATOM   962  C  CA  . TRP   A 1 124 ? -25.365 42.612 38.516 1.000 19.848  ? 123 TRP   AAA CA  1 ? 
ATOM   963  C  C   . TRP   A 1 124 ? -26.420 43.445 37.786 1.000 21.442  ? 123 TRP   AAA C   1 ? 
ATOM   964  O  O   . TRP   A 1 124 ? -26.201 44.665 37.511 1.000 25.380  ? 123 TRP   AAA O   1 ? 
ATOM   965  C  CB  . TRP   A 1 124 ? -25.642 42.473 40.017 1.000 20.549  ? 123 TRP   AAA CB  1 ? 
ATOM   966  C  CG  . TRP   A 1 124 ? -25.692 43.766 40.797 1.000 19.035  ? 123 TRP   AAA CG  1 ? 
ATOM   967  C  CD1 . TRP   A 1 124 ? -24.648 44.294 41.487 1.000 20.943  ? 123 TRP   AAA CD1 1 ? 
ATOM   968  C  CD2 . TRP   A 1 124 ? -26.825 44.621 41.092 1.000 18.821  ? 123 TRP   AAA CD2 1 ? 
ATOM   969  N  NE1 . TRP   A 1 124 ? -25.038 45.398 42.177 1.000 21.577  ? 123 TRP   AAA NE1 1 ? 
ATOM   970  C  CE2 . TRP   A 1 124 ? -26.371 45.615 41.984 1.000 20.600  ? 123 TRP   AAA CE2 1 ? 
ATOM   971  C  CE3 . TRP   A 1 124 ? -28.184 44.592 40.772 1.000 22.704  ? 123 TRP   AAA CE3 1 ? 
ATOM   972  C  CZ2 . TRP   A 1 124 ? -27.194 46.662 42.434 1.000 23.581  ? 123 TRP   AAA CZ2 1 ? 
ATOM   973  C  CZ3 . TRP   A 1 124 ? -29.006 45.591 41.248 1.000 22.854  ? 123 TRP   AAA CZ3 1 ? 
ATOM   974  C  CH2 . TRP   A 1 124 ? -28.514 46.605 42.078 1.000 24.154  ? 123 TRP   AAA CH2 1 ? 
ATOM   975  N  N   . ASN   A 1 125 ? -27.507 42.774 37.452 1.000 22.472  ? 124 ASN   AAA N   1 ? 
ATOM   976  C  CA  . ASN   A 1 125 ? -28.593 43.269 36.589 1.000 21.757  ? 124 ASN   AAA CA  1 ? 
ATOM   977  C  C   . ASN   A 1 125 ? -29.477 44.204 37.406 1.000 22.999  ? 124 ASN   AAA C   1 ? 
ATOM   978  O  O   . ASN   A 1 125 ? -30.456 43.751 38.025 1.000 22.501  ? 124 ASN   AAA O   1 ? 
ATOM   979  C  CB  . ASN   A 1 125 ? -29.378 42.112 35.998 1.000 23.317  ? 124 ASN   AAA CB  1 ? 
ATOM   980  C  CG  . ASN   A 1 125 ? -30.372 42.550 34.958 1.000 26.445  ? 124 ASN   AAA CG  1 ? 
ATOM   981  O  OD1 . ASN   A 1 125 ? -30.815 43.693 34.962 1.000 27.472  ? 124 ASN   AAA OD1 1 ? 
ATOM   982  N  ND2 . ASN   A 1 125 ? -30.736 41.647 34.063 1.000 28.830  ? 124 ASN   AAA ND2 1 ? 
ATOM   983  N  N   . SER   A 1 126 ? -29.156 45.497 37.319 1.000 21.735  ? 125 SER   AAA N   1 ? 
ATOM   984  C  CA  . SER   A 1 126 ? -29.886 46.595 38.002 1.000 26.761  ? 125 SER   AAA CA  1 ? 
ATOM   985  C  C   . SER   A 1 126 ? -31.094 47.058 37.170 1.000 25.103  ? 125 SER   AAA C   1 ? 
ATOM   986  O  O   . SER   A 1 126 ? -31.887 47.890 37.687 1.000 28.516  ? 125 SER   AAA O   1 ? 
ATOM   987  C  CB  . SER   A 1 126 ? -28.910 47.697 38.315 1.000 26.104  ? 125 SER   AAA CB  1 ? 
ATOM   988  O  OG  . SER   A 1 126 ? -28.360 48.240 37.120 1.000 29.891  ? 125 SER   AAA OG  1 ? 
ATOM   989  N  N   . ALA   A 1 127 ? -31.271 46.553 35.939 1.000 28.940  ? 126 ALA   AAA N   1 ? 
ATOM   990  C  CA  . ALA   A 1 127 ? -32.492 46.807 35.136 1.000 34.891  ? 126 ALA   AAA CA  1 ? 
ATOM   991  C  C   . ALA   A 1 127 ? -33.641 45.990 35.748 1.000 29.376  ? 126 ALA   AAA C   1 ? 
ATOM   992  O  O   . ALA   A 1 127 ? -34.744 46.479 35.861 1.000 30.587  ? 126 ALA   AAA O   1 ? 
ATOM   993  C  CB  . ALA   A 1 127 ? -32.274 46.466 33.678 1.000 38.947  ? 126 ALA   AAA CB  1 ? 
ATOM   994  N  N   . LYS   A 1 128 ? -33.358 44.762 36.170 1.000 28.732  ? 127 LYS   AAA N   1 ? 
ATOM   995  C  CA  . LYS   A 1 128 ? -34.419 43.822 36.588 1.000 26.264  ? 127 LYS   AAA CA  1 ? 
ATOM   996  C  C   . LYS   A 1 128 ? -34.533 43.770 38.112 1.000 25.009  ? 127 LYS   AAA C   1 ? 
ATOM   997  O  O   . LYS   A 1 128 ? -35.645 43.489 38.597 1.000 28.737  ? 127 LYS   AAA O   1 ? 
ATOM   998  C  CB  . LYS   A 1 128 ? -34.113 42.447 35.986 1.000 32.086  ? 127 LYS   AAA CB  1 ? 
ATOM   999  C  CG  . LYS   A 1 128 ? -34.561 42.290 34.540 1.000 34.069  ? 127 LYS   AAA CG  1 ? 
ATOM   1000 C  CD  . LYS   A 1 128 ? -34.608 40.856 34.106 1.000 41.428  ? 127 LYS   AAA CD  1 ? 
ATOM   1001 C  CE  . LYS   A 1 128 ? -35.874 40.149 34.544 1.000 44.642  ? 127 LYS   AAA CE  1 ? 
ATOM   1002 N  NZ  . LYS   A 1 128 ? -35.847 38.730 34.105 1.000 40.967  ? 127 LYS   AAA NZ  1 ? 
ATOM   1003 N  N   . TYR   A 1 129 ? -33.420 43.944 38.832 1.000 25.675  ? 128 TYR   AAA N   1 ? 
ATOM   1004 C  CA  . TYR   A 1 129 ? -33.325 43.593 40.278 1.000 26.834  ? 128 TYR   AAA CA  1 ? 
ATOM   1005 C  C   . TYR   A 1 129 ? -32.844 44.826 41.019 1.000 24.419  ? 128 TYR   AAA C   1 ? 
ATOM   1006 O  O   . TYR   A 1 129 ? -32.243 45.725 40.348 1.000 25.033  ? 128 TYR   AAA O   1 ? 
ATOM   1007 C  CB  . TYR   A 1 129 ? -32.436 42.360 40.495 1.000 26.131  ? 128 TYR   AAA CB  1 ? 
ATOM   1008 C  CG  . TYR   A 1 129 ? -32.845 41.225 39.596 1.000 25.554  ? 128 TYR   AAA CG  1 ? 
ATOM   1009 C  CD1 . TYR   A 1 129 ? -34.110 40.651 39.706 1.000 27.972  ? 128 TYR   AAA CD1 1 ? 
ATOM   1010 C  CD2 . TYR   A 1 129 ? -31.985 40.730 38.637 1.000 23.689  ? 128 TYR   AAA CD2 1 ? 
ATOM   1011 C  CE1 . TYR   A 1 129 ? -34.529 39.641 38.848 1.000 29.429  ? 128 TYR   AAA CE1 1 ? 
ATOM   1012 C  CE2 . TYR   A 1 129 ? -32.410 39.778 37.741 1.000 22.429  ? 128 TYR   AAA CE2 1 ? 
ATOM   1013 C  CZ  . TYR   A 1 129 ? -33.657 39.179 37.882 1.000 28.840  ? 128 TYR   AAA CZ  1 ? 
ATOM   1014 O  OH  . TYR   A 1 129 ? -34.027 38.162 37.034 1.000 26.870  ? 128 TYR   AAA OH  1 ? 
ATOM   1015 N  N   . SER   A 1 130 ? -33.171 44.914 42.310 1.000 24.252  ? 129 SER   AAA N   1 ? 
ATOM   1016 C  CA  . SER   A 1 130 ? -32.896 46.147 43.079 1.000 28.521  ? 129 SER   AAA CA  1 ? 
ATOM   1017 C  C   . SER   A 1 130 ? -31.635 45.971 43.927 1.000 26.870  ? 129 SER   AAA C   1 ? 
ATOM   1018 O  O   . SER   A 1 130 ? -31.181 46.926 44.504 1.000 24.729  ? 129 SER   AAA O   1 ? 
ATOM   1019 C  CB  . SER   A 1 130 ? -34.077 46.551 43.878 1.000 34.209  ? 129 SER   AAA CB  1 ? 
ATOM   1020 O  OG  . SER   A 1 130 ? -34.383 45.580 44.840 1.000 40.633  ? 129 SER   AAA OG  1 ? 
ATOM   1021 N  N   . SER   A 1 131 ? -31.039 44.785 43.969 1.000 24.310  ? 130 SER   AAA N   1 ? 
ATOM   1022 C  CA  . SER   A 1 131 ? -29.819 44.565 44.781 1.000 21.982  ? 130 SER   AAA CA  1 ? 
ATOM   1023 C  C   . SER   A 1 131 ? -29.014 43.381 44.226 1.000 20.797  ? 130 SER   AAA C   1 ? 
ATOM   1024 O  O   . SER   A 1 131 ? -29.575 42.549 43.494 1.000 23.380  ? 130 SER   AAA O   1 ? 
ATOM   1025 C  CB  . SER   A 1 131 ? -30.182 44.302 46.222 1.000 23.261  ? 130 SER   AAA CB  1 ? 
ATOM   1026 O  OG  . SER   A 1 131 ? -30.681 42.980 46.361 1.000 25.416  ? 130 SER   AAA OG  1 ? 
ATOM   1027 N  N   . LEU   A 1 132 ? -27.727 43.372 44.524 1.000 20.805  ? 131 LEU   AAA N   1 ? 
ATOM   1028 C  CA  . LEU   A 1 132 ? -26.858 42.220 44.233 1.000 20.355  ? 131 LEU   AAA CA  1 ? 
ATOM   1029 C  C   . LEU   A 1 132 ? -27.448 40.944 44.888 1.000 21.969  ? 131 LEU   AAA C   1 ? 
ATOM   1030 O  O   . LEU   A 1 132 ? -27.560 39.927 44.203 1.000 21.985  ? 131 LEU   AAA O   1 ? 
ATOM   1031 C  CB  . LEU   A 1 132 ? -25.456 42.498 44.747 1.000 21.603  ? 131 LEU   AAA CB  1 ? 
ATOM   1032 C  CG  . LEU   A 1 132 ? -24.561 41.267 44.694 1.000 22.598  ? 131 LEU   AAA CG  1 ? 
ATOM   1033 C  CD1 . LEU   A 1 132 ? -24.354 40.805 43.246 1.000 21.617  ? 131 LEU   AAA CD1 1 ? 
ATOM   1034 C  CD2 . LEU   A 1 132 ? -23.238 41.534 45.422 1.000 27.323  ? 131 LEU   AAA CD2 1 ? 
ATOM   1035 N  N   . ALA   A 1 133 ? -27.879 41.019 46.138 1.000 22.513  ? 132 ALA   AAA N   1 ? 
ATOM   1036 C  CA  . ALA   A 1 133 ? -28.502 39.897 46.860 1.000 23.880  ? 132 ALA   AAA CA  1 ? 
ATOM   1037 C  C   . ALA   A 1 133 ? -29.676 39.318 46.056 1.000 23.609  ? 132 ALA   AAA C   1 ? 
ATOM   1038 O  O   . ALA   A 1 133 ? -29.803 38.077 46.047 1.000 26.988  ? 132 ALA   AAA O   1 ? 
ATOM   1039 C  CB  . ALA   A 1 133 ? -28.930 40.319 48.249 1.000 26.049  ? 132 ALA   AAA CB  1 ? 
ATOM   1040 N  N   . GLU   A 1 134 ? -30.539 40.139 45.466 1.000 25.653  ? 133 GLU   AAA N   1 ? 
ATOM   1041 C  CA  . GLU   A 1 134 ? -31.691 39.659 44.657 1.000 24.580  ? 133 GLU   AAA CA  1 ? 
ATOM   1042 C  C   . GLU   A 1 134 ? -31.182 39.053 43.342 1.000 22.213  ? 133 GLU   AAA C   1 ? 
ATOM   1043 O  O   . GLU   A 1 134 ? -31.655 37.964 42.940 1.000 24.598  ? 133 GLU   AAA O   1 ? 
ATOM   1044 C  CB  . GLU   A 1 134 ? -32.659 40.822 44.405 1.000 23.476  ? 133 GLU   AAA CB  1 ? 
ATOM   1045 C  CG  . GLU   A 1 134 ? -33.865 40.413 43.575 1.000 27.394  ? 133 GLU   AAA CG  1 ? 
ATOM   1046 C  CD  . GLU   A 1 134 ? -34.855 41.516 43.260 1.000 26.734  ? 133 GLU   AAA CD  1 ? 
ATOM   1047 O  OE1 . GLU   A 1 134 ? -34.536 42.697 43.568 1.000 28.014  ? 133 GLU   AAA OE1 1 ? 
ATOM   1048 O  OE2 . GLU   A 1 134 ? -35.941 41.202 42.737 1.000 31.730  ? 133 GLU   AAA OE2 1 ? 
ATOM   1049 N  N   . ALA   A 1 135 ? -30.232 39.703 42.686 1.000 20.756  ? 134 ALA   AAA N   1 ? 
ATOM   1050 C  CA  . ALA   A 1 135 ? -29.727 39.346 41.344 1.000 22.227  ? 134 ALA   AAA CA  1 ? 
ATOM   1051 C  C   . ALA   A 1 135 ? -28.930 38.016 41.358 1.000 21.497  ? 134 ALA   AAA C   1 ? 
ATOM   1052 O  O   . ALA   A 1 135 ? -28.938 37.338 40.319 1.000 23.010  ? 134 ALA   AAA O   1 ? 
ATOM   1053 C  CB  . ALA   A 1 135 ? -28.883 40.482 40.832 1.000 21.744  ? 134 ALA   AAA CB  1 ? 
ATOM   1054 N  N   . ALA   A 1 136 ? -28.188 37.728 42.427 1.000 20.838  ? 135 ALA   AAA N   1 ? 
ATOM   1055 C  CA  . ALA   A 1 136 ? -27.067 36.754 42.449 1.000 23.182  ? 135 ALA   AAA CA  1 ? 
ATOM   1056 C  C   . ALA   A 1 136 ? -27.553 35.334 42.129 1.000 23.619  ? 135 ALA   AAA C   1 ? 
ATOM   1057 O  O   . ALA   A 1 136 ? -26.773 34.569 41.542 1.000 25.413  ? 135 ALA   AAA O   1 ? 
ATOM   1058 C  CB  . ALA   A 1 136 ? -26.356 36.828 43.779 1.000 23.004  ? 135 ALA   AAA CB  1 ? 
ATOM   1059 N  N   . SER   A 1 137 ? -28.796 34.990 42.455 1.000 23.613  ? 136 SER   AAA N   1 ? 
ATOM   1060 C  CA  . SER   A 1 137 ? -29.312 33.607 42.279 1.000 25.279  ? 136 SER   AAA CA  1 ? 
ATOM   1061 C  C   . SER   A 1 137 ? -30.180 33.467 41.021 1.000 28.949  ? 136 SER   AAA C   1 ? 
ATOM   1062 O  O   . SER   A 1 137 ? -30.774 32.401 40.851 1.000 34.183  ? 136 SER   AAA O   1 ? 
ATOM   1063 C  CB  . SER   A 1 137 ? -30.084 33.195 43.509 1.000 27.982  ? 136 SER   AAA CB  1 ? 
ATOM   1064 O  OG  . SER   A 1 137 ? -31.240 34.029 43.667 1.000 29.132  ? 136 SER   AAA OG  1 ? 
ATOM   1065 N  N   . LYS   A 1 138 ? -30.336 34.513 40.224 1.000 23.798  ? 137 LYS   AAA N   1 ? 
ATOM   1066 C  CA  . LYS   A 1 138 ? -31.221 34.582 39.037 1.000 22.411  ? 137 LYS   AAA CA  1 ? 
ATOM   1067 C  C   . LYS   A 1 138 ? -30.410 34.293 37.773 1.000 24.222  ? 137 LYS   AAA C   1 ? 
ATOM   1068 O  O   . LYS   A 1 138 ? -29.262 34.769 37.670 1.000 23.625  ? 137 LYS   AAA O   1 ? 
ATOM   1069 C  CB  . LYS   A 1 138 ? -31.830 35.978 38.921 1.000 25.950  ? 137 LYS   AAA CB  1 ? 
ATOM   1070 C  CG  . LYS   A 1 138 ? -32.590 36.455 40.156 1.000 31.094  ? 137 LYS   AAA CG  1 ? 
ATOM   1071 C  CD  . LYS   A 1 138 ? -33.951 35.786 40.242 1.000 38.248  ? 137 LYS   AAA CD  1 ? 
ATOM   1072 C  CE  . LYS   A 1 138 ? -34.922 36.460 41.177 1.000 48.522  ? 137 LYS   AAA CE  1 ? 
ATOM   1073 N  NZ  . LYS   A 1 138 ? -34.672 36.037 42.570 1.000 55.365  ? 137 LYS   AAA NZ  1 ? 
ATOM   1074 N  N   . ALA   A 1 139 ? -30.987 33.539 36.837 1.000 24.782  ? 138 ALA   AAA N   1 ? 
ATOM   1075 C  CA  . ALA   A 1 139 ? -30.306 33.105 35.601 1.000 26.480  ? 138 ALA   AAA CA  1 ? 
ATOM   1076 C  C   . ALA   A 1 139 ? -29.690 34.293 34.869 1.000 24.006  ? 138 ALA   AAA C   1 ? 
ATOM   1077 O  O   . ALA   A 1 139 ? -28.596 34.145 34.341 1.000 27.369  ? 138 ALA   AAA O   1 ? 
ATOM   1078 C  CB  . ALA   A 1 139 ? -31.278 32.367 34.721 1.000 31.662  ? 138 ALA   AAA CB  1 ? 
ATOM   1079 N  N   . ASP   A 1 140 ? -30.406 35.420 34.839 1.000 24.253  ? 139 ASP   AAA N   1 ? 
ATOM   1080 C  CA  . ASP   A 1 140 ? -29.967 36.642 34.111 1.000 26.652  ? 139 ASP   AAA CA  1 ? 
ATOM   1081 C  C   . ASP   A 1 140 ? -29.384 37.677 35.083 1.000 26.941  ? 139 ASP   AAA C   1 ? 
ATOM   1082 O  O   . ASP   A 1 140 ? -29.301 38.863 34.711 1.000 26.981  ? 139 ASP   AAA O   1 ? 
ATOM   1083 C  CB  . ASP   A 1 140 ? -31.145 37.244 33.354 1.000 29.301  ? 139 ASP   AAA CB  1 ? 
ATOM   1084 C  CG  . ASP   A 1 140 ? -32.353 37.495 34.242 1.000 27.787  ? 139 ASP   AAA CG  1 ? 
ATOM   1085 O  OD1 . ASP   A 1 140 ? -32.221 37.295 35.487 1.000 23.929  ? 139 ASP   AAA OD1 1 ? 
ATOM   1086 O  OD2 . ASP   A 1 140 ? -33.413 37.888 33.683 1.000 35.073  ? 139 ASP   AAA OD2 1 ? 
ATOM   1087 N  N   . GLY   A 1 141 ? -28.995 37.262 36.280 1.000 22.862  ? 140 GLY   AAA N   1 ? 
ATOM   1088 C  CA  . GLY   A 1 141 ? -28.626 38.170 37.379 1.000 22.953  ? 140 GLY   AAA CA  1 ? 
ATOM   1089 C  C   . GLY   A 1 141 ? -27.246 38.793 37.266 1.000 21.868  ? 140 GLY   AAA C   1 ? 
ATOM   1090 O  O   . GLY   A 1 141 ? -27.098 39.947 37.698 1.000 23.806  ? 140 GLY   AAA O   1 ? 
ATOM   1091 N  N   . LEU   A 1 142 ? -26.249 38.049 36.805 1.000 20.460  ? 141 LEU   AAA N   1 ? 
ATOM   1092 C  CA  . LEU   A 1 142 ? -24.831 38.428 36.885 1.000 20.144  ? 141 LEU   AAA CA  1 ? 
ATOM   1093 C  C   . LEU   A 1 142 ? -24.201 38.391 35.504 1.000 21.370  ? 141 LEU   AAA C   1 ? 
ATOM   1094 O  O   . LEU   A 1 142 ? -24.639 37.595 34.663 1.000 21.845  ? 141 LEU   AAA O   1 ? 
ATOM   1095 C  CB  . LEU   A 1 142 ? -24.042 37.538 37.840 1.000 20.872  ? 141 LEU   AAA CB  1 ? 
ATOM   1096 C  CG  . LEU   A 1 142 ? -24.553 37.420 39.274 1.000 19.840  ? 141 LEU   AAA CG  1 ? 
ATOM   1097 C  CD1 . LEU   A 1 142 ? -23.589 36.562 40.075 1.000 23.968  ? 141 LEU   AAA CD1 1 ? 
ATOM   1098 C  CD2 . LEU   A 1 142 ? -24.716 38.789 39.920 1.000 19.882  ? 141 LEU   AAA CD2 1 ? 
ATOM   1099 N  N   . ALA   A 1 143 ? -23.251 39.308 35.280 1.000 20.839  ? 142 ALA   AAA N   1 ? 
ATOM   1100 C  CA  . ALA   A 1 143 ? -22.409 39.396 34.070 1.000 20.036  ? 142 ALA   AAA CA  1 ? 
ATOM   1101 C  C   . ALA   A 1 143 ? -20.966 39.549 34.539 1.000 19.503  ? 142 ALA   AAA C   1 ? 
ATOM   1102 O  O   . ALA   A 1 143 ? -20.660 40.470 35.344 1.000 19.361  ? 142 ALA   AAA O   1 ? 
ATOM   1103 C  CB  . ALA   A 1 143 ? -22.845 40.553 33.195 1.000 23.829  ? 142 ALA   AAA CB  1 ? 
ATOM   1104 N  N   . VAL   A 1 144 ? -20.095 38.639 34.134 1.000 17.447  ? 143 VAL   AAA N   1 ? 
ATOM   1105 C  CA  . VAL   A 1 144 ? -18.666 38.706 34.498 1.000 17.548  ? 143 VAL   AAA CA  1 ? 
ATOM   1106 C  C   . VAL   A 1 144 ? -17.845 38.689 33.209 1.000 18.188  ? 143 VAL   AAA C   1 ? 
ATOM   1107 O  O   . VAL   A 1 144 ? -18.055 37.819 32.328 1.000 19.644  ? 143 VAL   AAA O   1 ? 
ATOM   1108 C  CB  . VAL   A 1 144 ? -18.250 37.558 35.425 1.000 18.385  ? 143 VAL   AAA CB  1 ? 
ATOM   1109 C  CG1 . VAL   A 1 144 ? -16.813 37.720 35.839 1.000 19.372  ? 143 VAL   AAA CG1 1 ? 
ATOM   1110 C  CG2 . VAL   A 1 144 ? -19.140 37.445 36.648 1.000 18.945  ? 143 VAL   AAA CG2 1 ? 
ATOM   1111 N  N   . ILE   A 1 145 ? -16.973 39.684 33.103 1.000 17.402  ? 144 ILE   AAA N   1 ? 
ATOM   1112 C  CA  . ILE   A 1 145 ? -15.958 39.772 32.024 1.000 17.258  ? 144 ILE   AAA CA  1 ? 
ATOM   1113 C  C   . ILE   A 1 145 ? -14.752 39.015 32.559 1.000 18.242  ? 144 ILE   AAA C   1 ? 
ATOM   1114 O  O   . ILE   A 1 145 ? -14.275 39.335 33.687 1.000 18.367  ? 144 ILE   AAA O   1 ? 
ATOM   1115 C  CB  . ILE   A 1 145 ? -15.559 41.228 31.703 1.000 18.292  ? 144 ILE   AAA CB  1 ? 
ATOM   1116 C  CG1 . ILE   A 1 145 ? -16.757 42.060 31.234 1.000 18.601  ? 144 ILE   AAA CG1 1 ? 
ATOM   1117 C  CG2 . ILE   A 1 145 ? -14.461 41.221 30.663 1.000 21.415  ? 144 ILE   AAA CG2 1 ? 
ATOM   1118 C  CD1 . ILE   A 1 145 ? -16.447 43.560 31.070 1.000 21.417  ? 144 ILE   AAA CD1 1 ? 
ATOM   1119 N  N   . GLY   A 1 146 ? -14.270 38.049 31.783 1.000 19.099  ? 145 GLY   AAA N   1 ? 
ATOM   1120 C  CA  . GLY   A 1 146 ? -12.993 37.396 32.073 1.000 18.709  ? 145 GLY   AAA CA  1 ? 
ATOM   1121 C  C   . GLY   A 1 146 ? -11.950 37.746 31.038 1.000 18.416  ? 145 GLY   AAA C   1 ? 
ATOM   1122 O  O   . GLY   A 1 146 ? -12.243 37.745 29.807 1.000 18.763  ? 145 GLY   AAA O   1 ? 
ATOM   1123 N  N   . VAL   A 1 147 ? -10.755 38.036 31.536 1.000 17.944  ? 146 VAL   AAA N   1 ? 
ATOM   1124 C  CA  . VAL   A 1 147 ? -9.576  38.363 30.708 1.000 17.352  ? 146 VAL   AAA CA  1 ? 
ATOM   1125 C  C   . VAL   A 1 147 ? -8.476  37.404 31.110 1.000 16.041  ? 146 VAL   AAA C   1 ? 
ATOM   1126 O  O   . VAL   A 1 147 ? -8.109  37.363 32.290 1.000 18.813  ? 146 VAL   AAA O   1 ? 
ATOM   1127 C  CB  . VAL   A 1 147 ? -9.136  39.829 30.895 1.000 18.049  ? 146 VAL   AAA CB  1 ? 
ATOM   1128 C  CG1 . VAL   A 1 147 ? -8.006  40.162 29.952 1.000 19.478  ? 146 VAL   AAA CG1 1 ? 
ATOM   1129 C  CG2 . VAL   A 1 147 ? -10.316 40.779 30.756 1.000 21.217  ? 146 VAL   AAA CG2 1 ? 
ATOM   1130 N  N   . LEU   A 1 148 ? -8.013  36.649 30.128 1.000 18.149  ? 147 LEU   AAA N   1 ? 
ATOM   1131 C  CA  . LEU   A 1 148 ? -6.889  35.724 30.323 1.000 20.343  ? 147 LEU   AAA CA  1 ? 
ATOM   1132 C  C   . LEU   A 1 148 ? -5.615  36.534 30.449 1.000 18.664  ? 147 LEU   AAA C   1 ? 
ATOM   1133 O  O   . LEU   A 1 148 ? -5.422  37.492 29.638 1.000 20.454  ? 147 LEU   AAA O   1 ? 
ATOM   1134 C  CB  . LEU   A 1 148 ? -6.878  34.770 29.127 1.000 19.663  ? 147 LEU   AAA CB  1 ? 
ATOM   1135 C  CG  . LEU   A 1 148 ? -8.127  33.894 29.081 1.000 24.987  ? 147 LEU   AAA CG  1 ? 
ATOM   1136 C  CD1 . LEU   A 1 148 ? -8.321  33.280 27.723 1.000 28.537  ? 147 LEU   AAA CD1 1 ? 
ATOM   1137 C  CD2 . LEU   A 1 148 ? -8.060  32.861 30.177 1.000 23.449  ? 147 LEU   AAA CD2 1 ? 
ATOM   1138 N  N   . MET   A 1 149 ? -4.788  36.171 31.421 1.000 17.404  ? 148 MET   AAA N   1 ? 
ATOM   1139 C  CA  . MET   A 1 149 ? -3.527  36.874 31.691 1.000 17.484  ? 148 MET   AAA CA  1 ? 
ATOM   1140 C  C   . MET   A 1 149 ? -2.349  35.979 31.310 1.000 18.345  ? 148 MET   AAA C   1 ? 
ATOM   1141 O  O   . MET   A 1 149 ? -2.200  34.902 31.907 1.000 19.599  ? 148 MET   AAA O   1 ? 
ATOM   1142 C  CB  . MET   A 1 149 ? -3.504  37.321 33.158 1.000 20.166  ? 148 MET   AAA CB  1 ? 
ATOM   1143 C  CG  . MET   A 1 149 ? -4.638  38.332 33.457 1.000 19.027  ? 148 MET   AAA CG  1 ? 
ATOM   1144 S  SD  . MET   A 1 149 ? -4.829  38.721 35.196 1.000 19.431  ? 148 MET   AAA SD  1 ? 
ATOM   1145 C  CE  . MET   A 1 149 ? -3.299  39.574 35.541 1.000 21.105  ? 148 MET   AAA CE  1 ? 
ATOM   1146 N  N   . LYS   A 1 150 ? -1.563  36.424 30.337 1.000 19.853  ? 149 LYS   AAA N   1 ? 
ATOM   1147 C  CA  A LYS   A 1 150 ? -0.440  35.649 29.757 0.500 20.673  ? 149 LYS   AAA CA  1 ? 
ATOM   1148 C  CA  B LYS   A 1 150 ? -0.443  35.644 29.769 0.500 20.740  ? 149 LYS   AAA CA  1 ? 
ATOM   1149 C  C   . LYS   A 1 150 ? 0.874   36.127 30.382 1.000 20.250  ? 149 LYS   AAA C   1 ? 
ATOM   1150 O  O   . LYS   A 1 150 ? 1.182   37.379 30.305 1.000 20.617  ? 149 LYS   AAA O   1 ? 
ATOM   1151 C  CB  A LYS   A 1 150 ? -0.394  35.790 28.234 0.500 22.060  ? 149 LYS   AAA CB  1 ? 
ATOM   1152 C  CB  B LYS   A 1 150 ? -0.411  35.768 28.248 0.500 22.902  ? 149 LYS   AAA CB  1 ? 
ATOM   1153 C  CG  A LYS   A 1 150 ? 0.683   34.960 27.556 0.500 22.723  ? 149 LYS   AAA CG  1 ? 
ATOM   1154 C  CG  B LYS   A 1 150 ? 0.650   34.920 27.577 0.500 24.400  ? 149 LYS   AAA CG  1 ? 
ATOM   1155 C  CD  A LYS   A 1 150 ? 0.701   35.067 26.043 0.500 26.536  ? 149 LYS   AAA CD  1 ? 
ATOM   1156 C  CD  B LYS   A 1 150 ? 0.568   34.961 26.075 0.500 29.098  ? 149 LYS   AAA CD  1 ? 
ATOM   1157 C  CE  A LYS   A 1 150 ? 1.133   36.413 25.498 0.500 25.822  ? 149 LYS   AAA CE  1 ? 
ATOM   1158 C  CE  B LYS   A 1 150 ? 1.821   34.442 25.399 0.500 31.860  ? 149 LYS   AAA CE  1 ? 
ATOM   1159 N  NZ  A LYS   A 1 150 ? 2.586   36.689 25.665 0.500 30.880  ? 149 LYS   AAA NZ  1 ? 
ATOM   1160 N  NZ  B LYS   A 1 150 ? 1.982   32.977 25.524 0.500 38.035  ? 149 LYS   AAA NZ  1 ? 
ATOM   1161 N  N   . VAL   A 1 151 ? 1.614   35.208 30.979 1.000 23.047  ? 150 VAL   AAA N   1 ? 
ATOM   1162 C  CA  . VAL   A 1 151 ? 2.897   35.589 31.599 1.000 21.992  ? 150 VAL   AAA CA  1 ? 
ATOM   1163 C  C   . VAL   A 1 151 ? 3.790   36.181 30.503 1.000 20.207  ? 150 VAL   AAA C   1 ? 
ATOM   1164 O  O   . VAL   A 1 151 ? 3.819   35.684 29.391 1.000 23.453  ? 150 VAL   AAA O   1 ? 
ATOM   1165 C  CB  . VAL   A 1 151 ? 3.548   34.445 32.394 1.000 24.082  ? 150 VAL   AAA CB  1 ? 
ATOM   1166 C  CG1 . VAL   A 1 151 ? 4.003   33.271 31.520 1.000 26.191  ? 150 VAL   AAA CG1 1 ? 
ATOM   1167 C  CG2 . VAL   A 1 151 ? 4.695   34.971 33.249 1.000 26.000  ? 150 VAL   AAA CG2 1 ? 
ATOM   1168 N  N   . GLY   A 1 152 ? 4.433   37.309 30.819 1.000 23.328  ? 151 GLY   AAA N   1 ? 
ATOM   1169 C  CA  . GLY   A 1 152 ? 5.365   38.003 29.918 1.000 25.021  ? 151 GLY   AAA CA  1 ? 
ATOM   1170 C  C   . GLY   A 1 152 ? 5.780   39.328 30.537 1.000 25.544  ? 151 GLY   AAA C   1 ? 
ATOM   1171 O  O   . GLY   A 1 152 ? 6.240   39.326 31.693 1.000 28.152  ? 151 GLY   AAA O   1 ? 
ATOM   1172 N  N   . GLU   A 1 153 ? 5.623   40.429 29.801 1.000 26.916  ? 152 GLU   AAA N   1 ? 
ATOM   1173 C  CA  . GLU   A 1 153 ? 6.079   41.764 30.255 1.000 28.911  ? 152 GLU   AAA CA  1 ? 
ATOM   1174 C  C   . GLU   A 1 153 ? 5.244   42.174 31.479 1.000 28.543  ? 152 GLU   AAA C   1 ? 
ATOM   1175 O  O   . GLU   A 1 153 ? 4.033   41.847 31.530 1.000 25.931  ? 152 GLU   AAA O   1 ? 
ATOM   1176 C  CB  . GLU   A 1 153 ? 5.937   42.803 29.134 1.000 32.913  ? 152 GLU   AAA CB  1 ? 
ATOM   1177 C  CG  . GLU   A 1 153 ? 6.640   42.447 27.836 1.000 43.950  ? 152 GLU   AAA CG  1 ? 
ATOM   1178 C  CD  . GLU   A 1 153 ? 8.134   42.684 27.811 1.000 57.554  ? 152 GLU   AAA CD  1 ? 
ATOM   1179 O  OE1 . GLU   A 1 153 ? 8.743   42.727 28.901 1.000 67.366  ? 152 GLU   AAA OE1 1 ? 
ATOM   1180 O  OE2 . GLU   A 1 153 ? 8.681   42.834 26.696 1.000 78.250  ? 152 GLU   AAA OE2 1 ? 
ATOM   1181 N  N   . ALA   A 1 154 ? 5.851   42.902 32.420 1.000 26.476  ? 153 ALA   AAA N   1 ? 
ATOM   1182 C  CA  . ALA   A 1 154 ? 5.138   43.541 33.555 1.000 21.979  ? 153 ALA   AAA CA  1 ? 
ATOM   1183 C  C   . ALA   A 1 154 ? 4.022   44.433 32.987 1.000 24.624  ? 153 ALA   AAA C   1 ? 
ATOM   1184 O  O   . ALA   A 1 154 ? 4.246   45.090 31.961 1.000 24.285  ? 153 ALA   AAA O   1 ? 
ATOM   1185 C  CB  . ALA   A 1 154 ? 6.098   44.356 34.407 1.000 27.347  ? 153 ALA   AAA CB  1 ? 
ATOM   1186 N  N   . ASN   A 1 155 ? 2.862   44.404 33.632 1.000 21.217  ? 154 ASN   AAA N   1 ? 
ATOM   1187 C  CA  . ASN   A 1 155 ? 1.655   45.152 33.229 1.000 23.073  ? 154 ASN   AAA CA  1 ? 
ATOM   1188 C  C   . ASN   A 1 155 ? 1.554   46.377 34.132 1.000 22.777  ? 154 ASN   AAA C   1 ? 
ATOM   1189 O  O   . ASN   A 1 155 ? 1.220   46.249 35.305 1.000 23.243  ? 154 ASN   AAA O   1 ? 
ATOM   1190 C  CB  . ASN   A 1 155 ? 0.429   44.252 33.317 1.000 23.362  ? 154 ASN   AAA CB  1 ? 
ATOM   1191 C  CG  . ASN   A 1 155 ? -0.800  44.893 32.730 1.000 23.026  ? 154 ASN   AAA CG  1 ? 
ATOM   1192 O  OD1 . ASN   A 1 155 ? -0.924  46.121 32.715 1.000 27.142  ? 154 ASN   AAA OD1 1 ? 
ATOM   1193 N  ND2 . ASN   A 1 155 ? -1.724  44.097 32.262 1.000 22.975  ? 154 ASN   AAA ND2 1 ? 
ATOM   1194 N  N   . PRO   A 1 156 ? 1.955   47.587 33.670 1.000 25.688  ? 155 PRO   AAA N   1 ? 
ATOM   1195 C  CA  . PRO   A 1 156 ? 1.897   48.761 34.533 1.000 28.059  ? 155 PRO   AAA CA  1 ? 
ATOM   1196 C  C   . PRO   A 1 156 ? 0.479   49.090 35.036 1.000 26.318  ? 155 PRO   AAA C   1 ? 
ATOM   1197 O  O   . PRO   A 1 156 ? 0.368   49.659 36.109 1.000 29.741  ? 155 PRO   AAA O   1 ? 
ATOM   1198 C  CB  . PRO   A 1 156 ? 2.474   49.887 33.654 1.000 36.281  ? 155 PRO   AAA CB  1 ? 
ATOM   1199 C  CG  . PRO   A 1 156 ? 2.363   49.390 32.220 1.000 34.093  ? 155 PRO   AAA CG  1 ? 
ATOM   1200 C  CD  . PRO   A 1 156 ? 2.466   47.883 32.325 1.000 27.446  ? 155 PRO   AAA CD  1 ? 
ATOM   1201 N  N   . LYS   A 1 157 ? -0.571  48.683 34.312 1.000 27.294  ? 156 LYS   AAA N   1 ? 
ATOM   1202 C  CA  . LYS   A 1 157 ? -1.973  49.019 34.685 1.000 27.905  ? 156 LYS   AAA CA  1 ? 
ATOM   1203 C  C   . LYS   A 1 157 ? -2.335  48.259 35.973 1.000 22.511  ? 156 LYS   AAA C   1 ? 
ATOM   1204 O  O   . LYS   A 1 157 ? -3.283  48.656 36.643 1.000 27.642  ? 156 LYS   AAA O   1 ? 
ATOM   1205 C  CB  . LYS   A 1 157 ? -2.960  48.720 33.550 1.000 29.695  ? 156 LYS   AAA CB  1 ? 
ATOM   1206 C  CG  . LYS   A 1 157 ? -2.675  49.376 32.200 1.000 34.357  ? 156 LYS   AAA CG  1 ? 
ATOM   1207 C  CD  . LYS   A 1 157 ? -3.460  50.634 31.950 1.000 44.791  ? 156 LYS   AAA CD  1 ? 
ATOM   1208 C  CE  . LYS   A 1 157 ? -4.253  50.628 30.655 1.000 53.266  ? 156 LYS   AAA CE  1 ? 
ATOM   1209 N  NZ  . LYS   A 1 157 ? -3.393  50.474 29.462 1.000 58.270  ? 156 LYS   AAA NZ  1 ? 
ATOM   1210 N  N   . LEU   A 1 158 ? -1.593  47.204 36.333 1.000 22.048  ? 157 LEU   AAA N   1 ? 
ATOM   1211 C  CA  . LEU   A 1 158 ? -1.796  46.560 37.648 1.000 25.654  ? 157 LEU   AAA CA  1 ? 
ATOM   1212 C  C   . LEU   A 1 158 ? -1.173  47.342 38.814 1.000 30.789  ? 157 LEU   AAA C   1 ? 
ATOM   1213 O  O   . LEU   A 1 158 ? -1.457  46.852 39.936 1.000 27.048  ? 157 LEU   AAA O   1 ? 
ATOM   1214 C  CB  . LEU   A 1 158 ? -1.183  45.159 37.612 1.000 24.926  ? 157 LEU   AAA CB  1 ? 
ATOM   1215 C  CG  . LEU   A 1 158 ? -1.804  44.184 36.622 1.000 24.249  ? 157 LEU   AAA CG  1 ? 
ATOM   1216 C  CD1 . LEU   A 1 158 ? -1.062  42.867 36.661 1.000 25.745  ? 157 LEU   AAA CD1 1 ? 
ATOM   1217 C  CD2 . LEU   A 1 158 ? -3.282  43.968 36.907 1.000 30.407  ? 157 LEU   AAA CD2 1 ? 
ATOM   1218 N  N   . GLN   A 1 159 ? -0.570  48.572 38.666 1.000 26.306  ? 158 GLN   AAA N   1 ? 
ATOM   1219 C  CA  . GLN   A 1 159 ? 0.402   49.035 39.673 1.000 30.257  ? 158 GLN   AAA CA  1 ? 
ATOM   1220 C  C   . GLN   A 1 159 ? -0.383  49.370 40.938 1.000 28.649  ? 158 GLN   AAA C   1 ? 
ATOM   1221 O  O   . GLN   A 1 159 ? 0.071   48.963 42.011 1.000 33.508  ? 158 GLN   AAA O   1 ? 
ATOM   1222 C  CB  . GLN   A 1 159 ? 1.208   50.256 39.195 1.000 32.258  ? 158 GLN   AAA CB  1 ? 
ATOM   1223 C  CG  . GLN   A 1 159 ? 2.418   50.567 40.065 1.000 36.260  ? 158 GLN   AAA CG  1 ? 
ATOM   1224 C  CD  . GLN   A 1 159 ? 3.351   49.374 40.173 1.000 43.917  ? 158 GLN   AAA CD  1 ? 
ATOM   1225 O  OE1 . GLN   A 1 159 ? 3.780   48.774 39.171 1.000 48.504  ? 158 GLN   AAA OE1 1 ? 
ATOM   1226 N  NE2 . GLN   A 1 159 ? 3.669   49.012 41.407 1.000 44.064  ? 158 GLN   AAA NE2 1 ? 
ATOM   1227 N  N   . LYS   A 1 160 ? -1.497  50.107 40.806 1.000 24.444  ? 159 LYS   AAA N   1 ? 
ATOM   1228 C  CA  . LYS   A 1 160 ? -2.271  50.546 41.976 1.000 24.073  ? 159 LYS   AAA CA  1 ? 
ATOM   1229 C  C   . LYS   A 1 160 ? -2.735  49.300 42.721 1.000 22.460  ? 159 LYS   AAA C   1 ? 
ATOM   1230 O  O   . LYS   A 1 160 ? -2.627  49.277 43.957 1.000 25.694  ? 159 LYS   AAA O   1 ? 
ATOM   1231 C  CB  . LYS   A 1 160 ? -3.422  51.488 41.599 1.000 29.595  ? 159 LYS   AAA CB  1 ? 
ATOM   1232 C  CG  . LYS   A 1 160 ? -4.222  51.999 42.792 1.000 33.673  ? 159 LYS   AAA CG  1 ? 
ATOM   1233 C  CD  . LYS   A 1 160 ? -5.517  52.706 42.422 1.000 35.805  ? 159 LYS   AAA CD  1 ? 
ATOM   1234 C  CE  . LYS   A 1 160 ? -6.345  53.042 43.645 1.000 31.992  ? 159 LYS   AAA CE  1 ? 
ATOM   1235 N  NZ  . LYS   A 1 160 ? -5.755  54.195 44.352 1.000 42.917  ? 159 LYS   AAA NZ  1 ? 
ATOM   1236 N  N   . VAL   A 1 161 ? -3.103  48.224 41.993 1.000 23.996  ? 160 VAL   AAA N   1 ? 
ATOM   1237 C  CA  . VAL   A 1 161 ? -3.696  47.046 42.690 1.000 22.406  ? 160 VAL   AAA CA  1 ? 
ATOM   1238 C  C   . VAL   A 1 161 ? -2.578  46.396 43.495 1.000 19.249  ? 160 VAL   AAA C   1 ? 
ATOM   1239 O  O   . VAL   A 1 161 ? -2.761  46.185 44.710 1.000 24.713  ? 160 VAL   AAA O   1 ? 
ATOM   1240 C  CB  . VAL   A 1 161 ? -4.362  46.040 41.740 1.000 24.140  ? 160 VAL   AAA CB  1 ? 
ATOM   1241 C  CG1 . VAL   A 1 161 ? -4.871  44.827 42.511 1.000 31.382  ? 160 VAL   AAA CG1 1 ? 
ATOM   1242 C  CG2 . VAL   A 1 161 ? -5.480  46.647 40.911 1.000 24.737  ? 160 VAL   AAA CG2 1 ? 
ATOM   1243 N  N   . LEU   A 1 162 ? -1.463  46.133 42.823 1.000 23.805  ? 161 LEU   AAA N   1 ? 
ATOM   1244 C  CA  . LEU   A 1 162 ? -0.282  45.458 43.429 1.000 28.587  ? 161 LEU   AAA CA  1 ? 
ATOM   1245 C  C   . LEU   A 1 162 ? 0.255   46.287 44.591 1.000 24.925  ? 161 LEU   AAA C   1 ? 
ATOM   1246 O  O   . LEU   A 1 162 ? 0.531   45.680 45.613 1.000 25.660  ? 161 LEU   AAA O   1 ? 
ATOM   1247 C  CB  . LEU   A 1 162 ? 0.790   45.215 42.360 1.000 29.633  ? 161 LEU   AAA CB  1 ? 
ATOM   1248 C  CG  . LEU   A 1 162 ? 0.364   44.219 41.282 1.000 33.348  ? 161 LEU   AAA CG  1 ? 
ATOM   1249 C  CD1 . LEU   A 1 162 ? 1.379   44.175 40.146 1.000 43.588  ? 161 LEU   AAA CD1 1 ? 
ATOM   1250 C  CD2 . LEU   A 1 162 ? 0.158   42.825 41.865 1.000 32.175  ? 161 LEU   AAA CD2 1 ? 
ATOM   1251 N  N   . ASP   A 1 163 ? 0.323   47.624 44.451 1.000 27.978  ? 162 ASP   AAA N   1 ? 
ATOM   1252 C  CA  . ASP   A 1 163 ? 0.855   48.541 45.496 1.000 23.992  ? 162 ASP   AAA CA  1 ? 
ATOM   1253 C  C   . ASP   A 1 163 ? -0.041  48.458 46.735 1.000 23.426  ? 162 ASP   AAA C   1 ? 
ATOM   1254 O  O   . ASP   A 1 163 ? 0.491   48.701 47.825 1.000 26.767  ? 162 ASP   AAA O   1 ? 
ATOM   1255 C  CB  . ASP   A 1 163 ? 1.005   50.007 45.030 1.000 26.862  ? 162 ASP   AAA CB  1 ? 
ATOM   1256 C  CG  . ASP   A 1 163 ? 2.107   50.253 44.001 1.000 31.712  ? 162 ASP   AAA CG  1 ? 
ATOM   1257 O  OD1 . ASP   A 1 163 ? 3.017   49.381 43.864 1.000 39.238  ? 162 ASP   AAA OD1 1 ? 
ATOM   1258 O  OD2 . ASP   A 1 163 ? 2.063   51.322 43.332 1.000 38.413  ? 162 ASP   AAA OD2 1 ? 
ATOM   1259 N  N   . ALA   A 1 164 ? -1.322  48.073 46.591 1.000 20.588  ? 163 ALA   AAA N   1 ? 
ATOM   1260 C  CA  . ALA   A 1 164 ? -2.310  48.081 47.687 1.000 22.343  ? 163 ALA   AAA CA  1 ? 
ATOM   1261 C  C   . ALA   A 1 164 ? -2.191  46.795 48.530 1.000 20.901  ? 163 ALA   AAA C   1 ? 
ATOM   1262 O  O   . ALA   A 1 164 ? -2.643  46.810 49.680 1.000 21.278  ? 163 ALA   AAA O   1 ? 
ATOM   1263 C  CB  . ALA   A 1 164 ? -3.717  48.239 47.140 1.000 22.132  ? 163 ALA   AAA CB  1 ? 
ATOM   1264 N  N   . LEU   A 1 165 ? -1.588  45.723 48.011 1.000 25.384  ? 164 LEU   AAA N   1 ? 
ATOM   1265 C  CA  . LEU   A 1 165 ? -1.624  44.404 48.696 1.000 25.227  ? 164 LEU   AAA CA  1 ? 
ATOM   1266 C  C   . LEU   A 1 165 ? -0.842  44.429 50.021 1.000 21.302  ? 164 LEU   AAA C   1 ? 
ATOM   1267 O  O   . LEU   A 1 165 ? -1.252  43.681 50.960 1.000 21.334  ? 164 LEU   AAA O   1 ? 
ATOM   1268 C  CB  . LEU   A 1 165 ? -1.067  43.317 47.777 1.000 23.477  ? 164 LEU   AAA CB  1 ? 
ATOM   1269 C  CG  . LEU   A 1 165 ? -1.841  43.018 46.497 1.000 21.897  ? 164 LEU   AAA CG  1 ? 
ATOM   1270 C  CD1 . LEU   A 1 165 ? -1.269  41.800 45.792 1.000 26.676  ? 164 LEU   AAA CD1 1 ? 
ATOM   1271 C  CD2 . LEU   A 1 165 ? -3.334  42.862 46.753 1.000 24.709  ? 164 LEU   AAA CD2 1 ? 
ATOM   1272 N  N   . GLN   A 1 166 ? 0.224   45.243 50.138 1.000 21.702  ? 165 GLN   AAA N   1 ? 
ATOM   1273 C  CA  . GLN   A 1 166 ? 1.037   45.296 51.389 1.000 20.821  ? 165 GLN   AAA CA  1 ? 
ATOM   1274 C  C   . GLN   A 1 166 ? 0.170   45.703 52.593 1.000 20.083  ? 165 GLN   AAA C   1 ? 
ATOM   1275 O  O   . GLN   A 1 166 ? 0.633   45.461 53.719 1.000 23.411  ? 165 GLN   AAA O   1 ? 
ATOM   1276 C  CB  . GLN   A 1 166 ? 2.247   46.231 51.295 1.000 28.722  ? 165 GLN   AAA CB  1 ? 
ATOM   1277 C  CG  . GLN   A 1 166 ? 1.941   47.602 50.703 1.000 34.418  ? 165 GLN   AAA CG  1 ? 
ATOM   1278 C  CD  . GLN   A 1 166 ? 1.205   48.532 51.643 1.000 35.341  ? 165 GLN   AAA CD  1 ? 
ATOM   1279 O  OE1 . GLN   A 1 166 ? 1.461   48.564 52.847 1.000 39.462  ? 165 GLN   AAA OE1 1 ? 
ATOM   1280 N  NE2 . GLN   A 1 166 ? 0.289   49.338 51.098 1.000 48.847  ? 165 GLN   AAA NE2 1 ? 
ATOM   1281 N  N   . ALA   A 1 167 ? -1.018  46.308 52.391 1.000 24.173  ? 166 ALA   AAA N   1 ? 
ATOM   1282 C  CA  . ALA   A 1 167 ? -1.872  46.794 53.501 1.000 22.801  ? 166 ALA   AAA CA  1 ? 
ATOM   1283 C  C   . ALA   A 1 167 ? -2.954  45.778 53.843 1.000 21.450  ? 166 ALA   AAA C   1 ? 
ATOM   1284 O  O   . ALA   A 1 167 ? -3.647  46.002 54.839 1.000 21.835  ? 166 ALA   AAA O   1 ? 
ATOM   1285 C  CB  . ALA   A 1 167 ? -2.484  48.148 53.193 1.000 28.115  ? 166 ALA   AAA CB  1 ? 
ATOM   1286 N  N   . ILE   A 1 168 ? -3.072  44.702 53.059 1.000 20.545  ? 167 ILE   AAA N   1 ? 
ATOM   1287 C  CA  . ILE   A 1 168 ? -4.127  43.673 53.279 1.000 21.932  ? 167 ILE   AAA CA  1 ? 
ATOM   1288 C  C   . ILE   A 1 168 ? -3.459  42.304 53.233 1.000 18.968  ? 167 ILE   AAA C   1 ? 
ATOM   1289 O  O   . ILE   A 1 168 ? -3.985  41.408 52.514 1.000 23.345  ? 167 ILE   AAA O   1 ? 
ATOM   1290 C  CB  . ILE   A 1 168 ? -5.267  43.774 52.255 1.000 21.343  ? 167 ILE   AAA CB  1 ? 
ATOM   1291 C  CG1 . ILE   A 1 168 ? -4.810  43.674 50.796 1.000 21.578  ? 167 ILE   AAA CG1 1 ? 
ATOM   1292 C  CG2 . ILE   A 1 168 ? -6.053  45.024 52.500 1.000 23.605  ? 167 ILE   AAA CG2 1 ? 
ATOM   1293 C  CD1 . ILE   A 1 168 ? -5.845  42.998 49.933 1.000 24.240  ? 167 ILE   AAA CD1 1 ? 
ATOM   1294 N  N   . LYS   A 1 169 ? -2.317  42.159 53.892 1.000 18.988  ? 168 LYS   AAA N   1 ? 
ATOM   1295 C  CA  . LYS   A 1 169 ? -1.489  40.939 53.708 1.000 20.837  ? 168 LYS   AAA CA  1 ? 
ATOM   1296 C  C   . LYS   A 1 169 ? -2.206  39.707 54.245 1.000 20.897  ? 168 LYS   AAA C   1 ? 
ATOM   1297 O  O   . LYS   A 1 169 ? -1.978  38.619 53.682 1.000 19.564  ? 168 LYS   AAA O   1 ? 
ATOM   1298 C  CB  . LYS   A 1 169 ? -0.123  41.088 54.363 1.000 22.872  ? 168 LYS   AAA CB  1 ? 
ATOM   1299 C  CG  . LYS   A 1 169 ? 0.921   41.676 53.422 1.000 29.864  ? 168 LYS   AAA CG  1 ? 
ATOM   1300 C  CD  . LYS   A 1 169 ? 1.126   40.754 52.237 1.000 41.880  ? 168 LYS   AAA CD  1 ? 
ATOM   1301 C  CE  . LYS   A 1 169 ? 2.462   40.905 51.563 1.000 44.977  ? 168 LYS   AAA CE  1 ? 
ATOM   1302 N  NZ  . LYS   A 1 169 ? 2.581   39.914 50.475 1.000 42.642  ? 168 LYS   AAA NZ  1 ? 
ATOM   1303 N  N   . THR   A 1 170 ? -2.967  39.834 55.312 1.000 20.479  ? 169 THR   AAA N   1 ? 
ATOM   1304 C  CA  . THR   A 1 170 ? -3.587  38.672 56.007 1.000 20.770  ? 169 THR   AAA CA  1 ? 
ATOM   1305 C  C   . THR   A 1 170 ? -5.106  38.753 55.931 1.000 21.771  ? 169 THR   AAA C   1 ? 
ATOM   1306 O  O   . THR   A 1 170 ? -5.692  39.839 55.639 1.000 22.352  ? 169 THR   AAA O   1 ? 
ATOM   1307 C  CB  . THR   A 1 170 ? -3.068  38.551 57.446 1.000 22.199  ? 169 THR   AAA CB  1 ? 
ATOM   1308 O  OG1 . THR   A 1 170 ? -3.254  39.794 58.103 1.000 23.050  ? 169 THR   AAA OG1 1 ? 
ATOM   1309 C  CG2 . THR   A 1 170 ? -1.605  38.167 57.511 1.000 21.582  ? 169 THR   AAA CG2 1 ? 
ATOM   1310 N  N   . LYS   A 1 171 ? -5.731  37.617 56.184 1.000 19.685  ? 170 LYS   AAA N   1 ? 
ATOM   1311 C  CA  . LYS   A 1 171 ? -7.160  37.383 55.950 1.000 22.057  ? 170 LYS   AAA CA  1 ? 
ATOM   1312 C  C   . LYS   A 1 171 ? -8.002  38.339 56.781 1.000 20.148  ? 170 LYS   AAA C   1 ? 
ATOM   1313 O  O   . LYS   A 1 171 ? -7.792  38.397 58.015 1.000 22.439  ? 170 LYS   AAA O   1 ? 
ATOM   1314 C  CB  . LYS   A 1 171 ? -7.538  35.968 56.372 1.000 23.464  ? 170 LYS   AAA CB  1 ? 
ATOM   1315 C  CG  . LYS   A 1 171 ? -9.016  35.672 56.189 1.000 23.724  ? 170 LYS   AAA CG  1 ? 
ATOM   1316 C  CD  . LYS   A 1 171 ? -9.352  34.242 56.382 1.000 28.179  ? 170 LYS   AAA CD  1 ? 
ATOM   1317 C  CE  . LYS   A 1 171 ? -10.853 34.038 56.239 1.000 38.457  ? 170 LYS   AAA CE  1 ? 
ATOM   1318 N  NZ  . LYS   A 1 171 ? -11.256 32.615 56.343 1.000 49.676  ? 170 LYS   AAA NZ  1 ? 
ATOM   1319 N  N   . GLY   A 1 172 ? -8.950  39.027 56.151 1.000 23.343  ? 171 GLY   AAA N   1 ? 
ATOM   1320 C  CA  . GLY   A 1 172 ? -9.842  39.925 56.895 1.000 21.816  ? 171 GLY   AAA CA  1 ? 
ATOM   1321 C  C   . GLY   A 1 172 ? -9.376  41.366 56.838 1.000 22.132  ? 171 GLY   AAA C   1 ? 
ATOM   1322 O  O   . GLY   A 1 172 ? -10.209 42.240 57.122 1.000 28.045  ? 171 GLY   AAA O   1 ? 
ATOM   1323 N  N   . LYS   A 1 173 ? -8.104  41.622 56.532 1.000 20.188  ? 172 LYS   AAA N   1 ? 
ATOM   1324 C  CA  . LYS   A 1 173 ? -7.605  43.016 56.390 1.000 19.711  ? 172 LYS   AAA CA  1 ? 
ATOM   1325 C  C   . LYS   A 1 173 ? -8.282  43.656 55.189 1.000 20.818  ? 172 LYS   AAA C   1 ? 
ATOM   1326 O  O   . LYS   A 1 173 ? -8.494  43.017 54.153 1.000 21.113  ? 172 LYS   AAA O   1 ? 
ATOM   1327 C  CB  . LYS   A 1 173 ? -6.080  43.050 56.316 1.000 22.429  ? 172 LYS   AAA CB  1 ? 
ATOM   1328 C  CG  . LYS   A 1 173 ? -5.392  42.784 57.651 1.000 23.122  ? 172 LYS   AAA CG  1 ? 
ATOM   1329 C  CD  . LYS   A 1 173 ? -3.967  43.295 57.702 1.000 24.705  ? 172 LYS   AAA CD  1 ? 
ATOM   1330 C  CE  . LYS   A 1 173 ? -3.889  44.781 57.957 1.000 29.514  ? 172 LYS   AAA CE  1 ? 
ATOM   1331 N  NZ  . LYS   A 1 173 ? -2.507  45.289 57.821 1.000 30.774  ? 172 LYS   AAA NZ  1 ? 
ATOM   1332 N  N   . ARG   A 1 174 ? -8.508  44.960 55.312 1.000 22.921  ? 173 ARG   AAA N   1 ? 
ATOM   1333 C  CA  . ARG   A 1 174 ? -9.175  45.710 54.232 1.000 19.910  ? 173 ARG   AAA CA  1 ? 
ATOM   1334 C  C   . ARG   A 1 174 ? -8.703  47.161 54.337 1.000 20.350  ? 173 ARG   AAA C   1 ? 
ATOM   1335 O  O   . ARG   A 1 174 ? -8.212  47.575 55.408 1.000 24.260  ? 173 ARG   AAA O   1 ? 
ATOM   1336 C  CB  . ARG   A 1 174 ? -10.697 45.562 54.344 1.000 21.042  ? 173 ARG   AAA CB  1 ? 
ATOM   1337 C  CG  . ARG   A 1 174 ? -11.332 46.121 55.610 1.000 26.262  ? 173 ARG   AAA CG  1 ? 
ATOM   1338 C  CD  . ARG   A 1 174 ? -12.771 45.670 55.810 1.000 27.234  ? 173 ARG   AAA CD  1 ? 
ATOM   1339 N  NE  . ARG   A 1 174 ? -12.672 44.274 56.181 1.000 32.542  ? 173 ARG   AAA NE  1 ? 
ATOM   1340 C  CZ  . ARG   A 1 174 ? -13.514 43.299 55.857 1.000 36.254  ? 173 ARG   AAA CZ  1 ? 
ATOM   1341 N  NH1 . ARG   A 1 174 ? -14.626 43.516 55.166 1.000 36.098  ? 173 ARG   AAA NH1 1 ? 
ATOM   1342 N  NH2 . ARG   A 1 174 ? -13.212 42.082 56.247 1.000 38.859  ? 173 ARG   AAA NH2 1 ? 
ATOM   1343 N  N   . ALA   A 1 175 ? -8.785  47.870 53.214 1.000 20.311  ? 174 ALA   AAA N   1 ? 
ATOM   1344 C  CA  . ALA   A 1 175 ? -8.309  49.255 53.133 1.000 21.923  ? 174 ALA   AAA CA  1 ? 
ATOM   1345 C  C   . ALA   A 1 175 ? -9.142  49.978 52.097 1.000 22.756  ? 174 ALA   AAA C   1 ? 
ATOM   1346 O  O   . ALA   A 1 175 ? -9.607  49.415 51.107 1.000 22.105  ? 174 ALA   AAA O   1 ? 
ATOM   1347 C  CB  . ALA   A 1 175 ? -6.838  49.265 52.804 1.000 25.665  ? 174 ALA   AAA CB  1 ? 
ATOM   1348 N  N   . PRO   A 1 176 ? -9.246  51.332 52.232 1.000 25.029  ? 175 PRO   AAA N   1 ? 
ATOM   1349 C  CA  . PRO   A 1 176 ? -9.840  52.085 51.153 1.000 26.827  ? 175 PRO   AAA CA  1 ? 
ATOM   1350 C  C   . PRO   A 1 176 ? -9.024  51.906 49.867 1.000 27.038  ? 175 PRO   AAA C   1 ? 
ATOM   1351 O  O   . PRO   A 1 176 ? -7.768  51.791 49.915 1.000 28.663  ? 175 PRO   AAA O   1 ? 
ATOM   1352 C  CB  . PRO   A 1 176 ? -9.725  53.545 51.587 1.000 27.825  ? 175 PRO   AAA CB  1 ? 
ATOM   1353 C  CG  . PRO   A 1 176 ? -9.446  53.477 53.069 1.000 30.928  ? 175 PRO   AAA CG  1 ? 
ATOM   1354 C  CD  . PRO   A 1 176 ? -8.808  52.135 53.367 1.000 27.169  ? 175 PRO   AAA CD  1 ? 
ATOM   1355 N  N   . PHE   A 1 177 ? -9.796  51.883 48.740 1.000 24.557  ? 176 PHE   AAA N   1 ? 
ATOM   1356 C  CA  . PHE   A 1 177 ? -9.175  51.702 47.404 1.000 23.305  ? 176 PHE   AAA CA  1 ? 
ATOM   1357 C  C   . PHE   A 1 177 ? -10.031 52.488 46.441 1.000 21.486  ? 176 PHE   AAA C   1 ? 
ATOM   1358 O  O   . PHE   A 1 177 ? -11.161 52.096 46.196 1.000 23.691  ? 176 PHE   AAA O   1 ? 
ATOM   1359 C  CB  . PHE   A 1 177 ? -9.130  50.224 47.018 1.000 21.937  ? 176 PHE   AAA CB  1 ? 
ATOM   1360 C  CG  . PHE   A 1 177 ? -8.417  49.981 45.719 1.000 22.138  ? 176 PHE   AAA CG  1 ? 
ATOM   1361 C  CD1 . PHE   A 1 177 ? -9.094  50.129 44.505 1.000 23.514  ? 176 PHE   AAA CD1 1 ? 
ATOM   1362 C  CD2 . PHE   A 1 177 ? -7.070  49.597 45.708 1.000 24.282  ? 176 PHE   AAA CD2 1 ? 
ATOM   1363 C  CE1 . PHE   A 1 177 ? -8.450  49.872 43.300 1.000 24.042  ? 176 PHE   AAA CE1 1 ? 
ATOM   1364 C  CE2 . PHE   A 1 177 ? -6.421  49.373 44.503 1.000 25.370  ? 176 PHE   AAA CE2 1 ? 
ATOM   1365 C  CZ  . PHE   A 1 177 ? -7.117  49.483 43.307 1.000 23.219  ? 176 PHE   AAA CZ  1 ? 
ATOM   1366 N  N   . THR   A 1 178 ? -9.560  53.696 46.111 1.000 21.888  ? 177 THR   AAA N   1 ? 
ATOM   1367 C  CA  . THR   A 1 178 ? -10.435 54.727 45.529 1.000 24.212  ? 177 THR   AAA CA  1 ? 
ATOM   1368 C  C   . THR   A 1 178 ? -9.858  55.231 44.205 1.000 20.739  ? 177 THR   AAA C   1 ? 
ATOM   1369 O  O   . THR   A 1 178 ? -8.663  55.027 43.893 1.000 24.100  ? 177 THR   AAA O   1 ? 
ATOM   1370 C  CB  . THR   A 1 178 ? -10.662 55.888 46.515 1.000 24.180  ? 177 THR   AAA CB  1 ? 
ATOM   1371 O  OG1 . THR   A 1 178 ? -9.416  56.519 46.824 1.000 27.762  ? 177 THR   AAA OG1 1 ? 
ATOM   1372 C  CG2 . THR   A 1 178 ? -11.306 55.472 47.817 1.000 25.927  ? 177 THR   AAA CG2 1 ? 
ATOM   1373 N  N   . ASN   A 1 179 ? -10.729 55.880 43.450 1.000 24.028  ? 178 ASN   AAA N   1 ? 
ATOM   1374 C  CA  . ASN   A 1 179 ? -10.328 56.652 42.262 1.000 23.567  ? 178 ASN   AAA CA  1 ? 
ATOM   1375 C  C   . ASN   A 1 179 ? -9.673  55.703 41.263 1.000 21.380  ? 178 ASN   AAA C   1 ? 
ATOM   1376 O  O   . ASN   A 1 179 ? -8.535  55.927 40.890 1.000 25.357  ? 178 ASN   AAA O   1 ? 
ATOM   1377 C  CB  . ASN   A 1 179 ? -9.427  57.825 42.655 1.000 24.151  ? 178 ASN   AAA CB  1 ? 
ATOM   1378 C  CG  . ASN   A 1 179 ? -9.277  58.780 41.490 1.000 29.765  ? 178 ASN   AAA CG  1 ? 
ATOM   1379 O  OD1 . ASN   A 1 179 ? -10.218 58.895 40.680 1.000 31.553  ? 178 ASN   AAA OD1 1 ? 
ATOM   1380 N  ND2 . ASN   A 1 179 ? -8.127  59.447 41.388 1.000 28.328  ? 178 ASN   AAA ND2 1 ? 
ATOM   1381 N  N   . PHE   A 1 180 ? -10.366 54.627 40.904 1.000 24.218  ? 179 PHE   AAA N   1 ? 
ATOM   1382 C  CA  . PHE   A 1 180 ? -9.800  53.587 40.012 1.000 23.184  ? 179 PHE   AAA CA  1 ? 
ATOM   1383 C  C   . PHE   A 1 180 ? -10.904 53.072 39.058 1.000 25.206  ? 179 PHE   AAA C   1 ? 
ATOM   1384 O  O   . PHE   A 1 180 ? -12.018 52.693 39.524 1.000 23.972  ? 179 PHE   AAA O   1 ? 
ATOM   1385 C  CB  . PHE   A 1 180 ? -9.187  52.439 40.808 1.000 23.056  ? 179 PHE   AAA CB  1 ? 
ATOM   1386 C  CG  . PHE   A 1 180 ? -8.521  51.446 39.903 1.000 22.970  ? 179 PHE   AAA CG  1 ? 
ATOM   1387 C  CD1 . PHE   A 1 180 ? -7.270  51.718 39.373 1.000 24.727  ? 179 PHE   AAA CD1 1 ? 
ATOM   1388 C  CD2 . PHE   A 1 180 ? -9.146  50.258 39.567 1.000 23.518  ? 179 PHE   AAA CD2 1 ? 
ATOM   1389 C  CE1 . PHE   A 1 180 ? -6.639  50.840 38.515 1.000 26.299  ? 179 PHE   AAA CE1 1 ? 
ATOM   1390 C  CE2 . PHE   A 1 180 ? -8.540  49.425 38.653 1.000 23.460  ? 179 PHE   AAA CE2 1 ? 
ATOM   1391 C  CZ  . PHE   A 1 180 ? -7.274  49.676 38.189 1.000 23.771  ? 179 PHE   AAA CZ  1 ? 
ATOM   1392 N  N   . ASP   A 1 181 ? -10.567 53.161 37.769 1.000 27.562  ? 180 ASP   AAA N   1 ? 
ATOM   1393 C  CA  . ASP   A 1 181 ? -11.424 52.705 36.644 1.000 24.970  ? 180 ASP   AAA CA  1 ? 
ATOM   1394 C  C   . ASP   A 1 181 ? -10.865 51.372 36.128 1.000 24.536  ? 180 ASP   AAA C   1 ? 
ATOM   1395 O  O   . ASP   A 1 181 ? -9.859  51.354 35.393 1.000 26.642  ? 180 ASP   AAA O   1 ? 
ATOM   1396 C  CB  . ASP   A 1 181 ? -11.487 53.777 35.557 1.000 26.359  ? 180 ASP   AAA CB  1 ? 
ATOM   1397 C  CG  . ASP   A 1 181 ? -12.312 53.373 34.356 1.000 25.467  ? 180 ASP   AAA CG  1 ? 
ATOM   1398 O  OD1 . ASP   A 1 181 ? -12.769 52.184 34.334 1.000 24.096  ? 180 ASP   AAA OD1 1 ? 
ATOM   1399 O  OD2 . ASP   A 1 181 ? -12.522 54.243 33.469 1.000 31.900  ? 180 ASP   AAA OD2 1 ? 
ATOM   1400 N  N   . PRO   A 1 182 ? -11.506 50.205 36.431 1.000 21.041  ? 181 PRO   AAA N   1 ? 
ATOM   1401 C  CA  . PRO   A 1 182 ? -10.946 48.899 36.053 1.000 21.141  ? 181 PRO   AAA CA  1 ? 
ATOM   1402 C  C   . PRO   A 1 182 ? -11.030 48.626 34.550 1.000 21.839  ? 181 PRO   AAA C   1 ? 
ATOM   1403 O  O   . PRO   A 1 182 ? -10.414 47.708 34.099 1.000 23.453  ? 181 PRO   AAA O   1 ? 
ATOM   1404 C  CB  . PRO   A 1 182 ? -11.758 47.885 36.862 1.000 23.741  ? 181 PRO   AAA CB  1 ? 
ATOM   1405 C  CG  . PRO   A 1 182 ? -13.035 48.602 37.214 1.000 22.793  ? 181 PRO   AAA CG  1 ? 
ATOM   1406 C  CD  . PRO   A 1 182 ? -12.741 50.094 37.199 1.000 20.797  ? 181 PRO   AAA CD  1 ? 
ATOM   1407 N  N   . SER   A 1 183 ? -11.761 49.419 33.776 1.000 22.479  ? 182 SER   AAA N   1 ? 
ATOM   1408 C  CA  . SER   A 1 183 ? -11.740 49.308 32.290 1.000 22.268  ? 182 SER   AAA CA  1 ? 
ATOM   1409 C  C   . SER   A 1 183 ? -10.318 49.560 31.766 1.000 20.694  ? 182 SER   AAA C   1 ? 
ATOM   1410 O  O   . SER   A 1 183 ? -10.036 49.117 30.644 1.000 23.408  ? 182 SER   AAA O   1 ? 
ATOM   1411 C  CB  . SER   A 1 183 ? -12.770 50.219 31.621 1.000 26.478  ? 182 SER   AAA CB  1 ? 
ATOM   1412 O  OG  . SER   A 1 183 ? -12.395 51.563 31.748 1.000 28.658  ? 182 SER   AAA OG  1 ? 
ATOM   1413 N  N   . THR   A 1 184 ? -9.425  50.195 32.552 1.000 20.829  ? 183 THR   AAA N   1 ? 
ATOM   1414 C  CA  . THR   A 1 184 ? -7.990  50.349 32.188 1.000 23.444  ? 183 THR   AAA CA  1 ? 
ATOM   1415 C  C   . THR   A 1 184 ? -7.252  49.000 32.182 1.000 20.603  ? 183 THR   AAA C   1 ? 
ATOM   1416 O  O   . THR   A 1 184 ? -6.137  48.922 31.670 1.000 24.703  ? 183 THR   AAA O   1 ? 
ATOM   1417 C  CB  . THR   A 1 184 ? -7.244  51.256 33.168 1.000 23.370  ? 183 THR   AAA CB  1 ? 
ATOM   1418 O  OG1 . THR   A 1 184 ? -7.337  50.804 34.520 1.000 23.975  ? 183 THR   AAA OG1 1 ? 
ATOM   1419 C  CG2 . THR   A 1 184 ? -7.782  52.681 33.115 1.000 24.582  ? 183 THR   AAA CG2 1 ? 
ATOM   1420 N  N   . LEU   A 1 185 ? -7.829  47.972 32.790 1.000 19.627  ? 184 LEU   AAA N   1 ? 
ATOM   1421 C  CA  . LEU   A 1 185 ? -7.184  46.641 32.852 1.000 21.261  ? 184 LEU   AAA CA  1 ? 
ATOM   1422 C  C   . LEU   A 1 185 ? -7.579  45.818 31.627 1.000 20.341  ? 184 LEU   AAA C   1 ? 
ATOM   1423 O  O   . LEU   A 1 185 ? -6.933  44.769 31.375 1.000 24.472  ? 184 LEU   AAA O   1 ? 
ATOM   1424 C  CB  . LEU   A 1 185 ? -7.647  45.925 34.112 1.000 19.482  ? 184 LEU   AAA CB  1 ? 
ATOM   1425 C  CG  . LEU   A 1 185 ? -7.176  46.531 35.423 1.000 21.330  ? 184 LEU   AAA CG  1 ? 
ATOM   1426 C  CD1 . LEU   A 1 185 ? -7.826  45.843 36.605 1.000 23.072  ? 184 LEU   AAA CD1 1 ? 
ATOM   1427 C  CD2 . LEU   A 1 185 ? -5.667  46.558 35.553 1.000 22.939  ? 184 LEU   AAA CD2 1 ? 
ATOM   1428 N  N   . LEU   A 1 186 ? -8.651  46.204 30.943 1.000 21.787  ? 185 LEU   AAA N   1 ? 
ATOM   1429 C  CA  . LEU   A 1 186 ? -9.164  45.423 29.789 1.000 21.994  ? 185 LEU   AAA CA  1 ? 
ATOM   1430 C  C   . LEU   A 1 186 ? -8.229  45.564 28.583 1.000 20.935  ? 185 LEU   AAA C   1 ? 
ATOM   1431 O  O   . LEU   A 1 186 ? -7.460  46.521 28.445 1.000 23.075  ? 185 LEU   AAA O   1 ? 
ATOM   1432 C  CB  . LEU   A 1 186 ? -10.602 45.834 29.469 1.000 24.840  ? 185 LEU   AAA CB  1 ? 
ATOM   1433 C  CG  . LEU   A 1 186 ? -11.619 45.664 30.598 1.000 24.346  ? 185 LEU   AAA CG  1 ? 
ATOM   1434 C  CD1 . LEU   A 1 186 ? -12.983 46.162 30.130 1.000 25.068  ? 185 LEU   AAA CD1 1 ? 
ATOM   1435 C  CD2 . LEU   A 1 186 ? -11.702 44.198 31.052 1.000 24.510  ? 185 LEU   AAA CD2 1 ? 
ATOM   1436 N  N   . PRO   A 1 187 ? -8.187  44.528 27.708 1.000 20.830  ? 186 PRO   AAA N   1 ? 
ATOM   1437 C  CA  . PRO   A 1 187 ? -7.411  44.568 26.473 1.000 21.748  ? 186 PRO   AAA CA  1 ? 
ATOM   1438 C  C   . PRO   A 1 187 ? -7.993  45.590 25.478 1.000 26.508  ? 186 PRO   AAA C   1 ? 
ATOM   1439 O  O   . PRO   A 1 187 ? -9.138  46.051 25.662 1.000 23.600  ? 186 PRO   AAA O   1 ? 
ATOM   1440 C  CB  . PRO   A 1 187 ? -7.466  43.101 25.989 1.000 22.554  ? 186 PRO   AAA CB  1 ? 
ATOM   1441 C  CG  . PRO   A 1 187 ? -8.791  42.589 26.521 1.000 23.853  ? 186 PRO   AAA CG  1 ? 
ATOM   1442 C  CD  . PRO   A 1 187 ? -8.999  43.313 27.844 1.000 20.111  ? 186 PRO   AAA CD  1 ? 
ATOM   1443 N  N   . SER   A 1 188 ? -7.185  45.982 24.490 1.000 27.667  ? 187 SER   AAA N   1 ? 
ATOM   1444 C  CA  . SER   A 1 188 ? -7.541  46.998 23.460 1.000 30.689  ? 187 SER   AAA CA  1 ? 
ATOM   1445 C  C   . SER   A 1 188 ? -8.782  46.551 22.686 1.000 26.116  ? 187 SER   AAA C   1 ? 
ATOM   1446 O  O   . SER   A 1 188 ? -9.684  47.372 22.518 1.000 34.854  ? 187 SER   AAA O   1 ? 
ATOM   1447 C  CB  . SER   A 1 188 ? -6.396  47.253 22.516 1.000 38.826  ? 187 SER   AAA CB  1 ? 
ATOM   1448 O  OG  . SER   A 1 188 ? -5.177  47.245 23.229 1.000 53.554  ? 187 SER   AAA OG  1 ? 
ATOM   1449 N  N   . SER   A 1 189 ? -8.797  45.282 22.254 1.000 28.728  ? 188 SER   AAA N   1 ? 
ATOM   1450 C  CA  . SER   A 1 189 ? -9.923  44.600 21.563 1.000 31.608  ? 188 SER   AAA CA  1 ? 
ATOM   1451 C  C   . SER   A 1 189 ? -10.868 44.032 22.616 1.000 24.806  ? 188 SER   AAA C   1 ? 
ATOM   1452 O  O   . SER   A 1 189 ? -10.334 43.402 23.596 1.000 26.089  ? 188 SER   AAA O   1 ? 
ATOM   1453 C  CB  . SER   A 1 189 ? -9.448  43.474 20.673 1.000 33.443  ? 188 SER   AAA CB  1 ? 
ATOM   1454 O  OG  . SER   A 1 189 ? -10.554 42.845 20.046 1.000 33.442  ? 188 SER   AAA OG  1 ? 
ATOM   1455 N  N   . LEU   A 1 190 ? -12.176 44.280 22.456 1.000 27.304  ? 189 LEU   AAA N   1 ? 
ATOM   1456 C  CA  . LEU   A 1 190 ? -13.228 43.718 23.341 1.000 28.318  ? 189 LEU   AAA CA  1 ? 
ATOM   1457 C  C   . LEU   A 1 190 ? -14.001 42.657 22.550 1.000 30.027  ? 189 LEU   AAA C   1 ? 
ATOM   1458 O  O   . LEU   A 1 190 ? -15.133 42.297 22.972 1.000 26.066  ? 189 LEU   AAA O   1 ? 
ATOM   1459 C  CB  . LEU   A 1 190 ? -14.111 44.845 23.907 1.000 28.654  ? 189 LEU   AAA CB  1 ? 
ATOM   1460 C  CG  . LEU   A 1 190 ? -13.388 45.802 24.870 1.000 33.159  ? 189 LEU   AAA CG  1 ? 
ATOM   1461 C  CD1 . LEU   A 1 190 ? -14.335 46.841 25.471 1.000 35.099  ? 189 LEU   AAA CD1 1 ? 
ATOM   1462 C  CD2 . LEU   A 1 190 ? -12.675 45.058 25.992 1.000 32.440  ? 189 LEU   AAA CD2 1 ? 
ATOM   1463 N  N   . ASP   A 1 191 ? -13.381 42.124 21.482 1.000 27.716  ? 190 ASP   AAA N   1 ? 
ATOM   1464 C  CA  . ASP   A 1 191 ? -13.857 40.882 20.815 1.000 26.237  ? 190 ASP   AAA CA  1 ? 
ATOM   1465 C  C   . ASP   A 1 191 ? -14.007 39.803 21.887 1.000 24.656  ? 190 ASP   AAA C   1 ? 
ATOM   1466 O  O   . ASP   A 1 191 ? -13.150 39.712 22.760 1.000 24.306  ? 190 ASP   AAA O   1 ? 
ATOM   1467 C  CB  . ASP   A 1 191 ? -12.893 40.392 19.734 1.000 26.630  ? 190 ASP   AAA CB  1 ? 
ATOM   1468 C  CG  . ASP   A 1 191 ? -12.982 41.127 18.410 1.000 31.369  ? 190 ASP   AAA CG  1 ? 
ATOM   1469 O  OD1 . ASP   A 1 191 ? -13.878 41.939 18.259 1.000 35.027  ? 190 ASP   AAA OD1 1 ? 
ATOM   1470 O  OD2 . ASP   A 1 191 ? -12.148 40.861 17.534 1.000 35.869  ? 190 ASP   AAA OD2 1 ? 
ATOM   1471 N  N   . PHE   A 1 192 ? -15.092 39.036 21.853 1.000 24.132  ? 191 PHE   AAA N   1 ? 
ATOM   1472 C  CA  . PHE   A 1 192 ? -15.403 38.170 23.009 1.000 21.360  ? 191 PHE   AAA CA  1 ? 
ATOM   1473 C  C   . PHE   A 1 192 ? -16.114 36.897 22.579 1.000 21.499  ? 191 PHE   AAA C   1 ? 
ATOM   1474 O  O   . PHE   A 1 192 ? -16.678 36.812 21.486 1.000 23.483  ? 191 PHE   AAA O   1 ? 
ATOM   1475 C  CB  . PHE   A 1 192 ? -16.210 38.909 24.076 1.000 23.368  ? 191 PHE   AAA CB  1 ? 
ATOM   1476 C  CG  . PHE   A 1 192 ? -17.591 39.290 23.634 1.000 23.002  ? 191 PHE   AAA CG  1 ? 
ATOM   1477 C  CD1 . PHE   A 1 192 ? -17.809 40.450 22.924 1.000 25.834  ? 191 PHE   AAA CD1 1 ? 
ATOM   1478 C  CD2 . PHE   A 1 192 ? -18.681 38.505 23.930 1.000 23.886  ? 191 PHE   AAA CD2 1 ? 
ATOM   1479 C  CE1 . PHE   A 1 192 ? -19.076 40.771 22.471 1.000 25.795  ? 191 PHE   AAA CE1 1 ? 
ATOM   1480 C  CE2 . PHE   A 1 192 ? -19.953 38.839 23.498 1.000 24.441  ? 191 PHE   AAA CE2 1 ? 
ATOM   1481 C  CZ  . PHE   A 1 192 ? -20.153 39.985 22.776 1.000 24.681  ? 191 PHE   AAA CZ  1 ? 
ATOM   1482 N  N   . TRP   A 1 193 ? -16.053 35.945 23.502 1.000 24.004  ? 192 TRP   AAA N   1 ? 
ATOM   1483 C  CA  . TRP   A 1 193 ? -16.959 34.780 23.572 1.000 25.688  ? 192 TRP   AAA CA  1 ? 
ATOM   1484 C  C   . TRP   A 1 193 ? -17.969 35.009 24.686 1.000 24.129  ? 192 TRP   AAA C   1 ? 
ATOM   1485 O  O   . TRP   A 1 193 ? -17.615 35.682 25.689 1.000 25.317  ? 192 TRP   AAA O   1 ? 
ATOM   1486 C  CB  . TRP   A 1 193 ? -16.138 33.524 23.854 1.000 20.617  ? 192 TRP   AAA CB  1 ? 
ATOM   1487 C  CG  . TRP   A 1 193 ? -15.141 33.177 22.798 1.000 21.088  ? 192 TRP   AAA CG  1 ? 
ATOM   1488 C  CD1 . TRP   A 1 193 ? -15.402 32.577 21.593 1.000 28.138  ? 192 TRP   AAA CD1 1 ? 
ATOM   1489 C  CD2 . TRP   A 1 193 ? -13.712 33.234 22.908 1.000 23.589  ? 192 TRP   AAA CD2 1 ? 
ATOM   1490 N  NE1 . TRP   A 1 193 ? -14.245 32.321 20.914 1.000 25.697  ? 192 TRP   AAA NE1 1 ? 
ATOM   1491 C  CE2 . TRP   A 1 193 ? -13.189 32.694 21.706 1.000 23.529  ? 192 TRP   AAA CE2 1 ? 
ATOM   1492 C  CE3 . TRP   A 1 193 ? -12.824 33.684 23.891 1.000 21.360  ? 192 TRP   AAA CE3 1 ? 
ATOM   1493 C  CZ2 . TRP   A 1 193 ? -11.821 32.598 21.479 1.000 23.181  ? 192 TRP   AAA CZ2 1 ? 
ATOM   1494 C  CZ3 . TRP   A 1 193 ? -11.469 33.569 23.668 1.000 20.163  ? 192 TRP   AAA CZ3 1 ? 
ATOM   1495 C  CH2 . TRP   A 1 193 ? -10.979 33.035 22.476 1.000 21.612  ? 192 TRP   AAA CH2 1 ? 
ATOM   1496 N  N   . THR   A 1 194 ? -19.161 34.439 24.554 1.000 20.984  ? 193 THR   AAA N   1 ? 
ATOM   1497 C  CA  . THR   A 1 194 ? -20.129 34.423 25.663 1.000 22.223  ? 193 THR   AAA CA  1 ? 
ATOM   1498 C  C   . THR   A 1 194 ? -20.785 33.040 25.783 1.000 22.334  ? 193 THR   AAA C   1 ? 
ATOM   1499 O  O   . THR   A 1 194 ? -21.038 32.362 24.744 1.000 23.877  ? 193 THR   AAA O   1 ? 
ATOM   1500 C  CB  . THR   A 1 194 ? -21.153 35.549 25.511 1.000 21.692  ? 193 THR   AAA CB  1 ? 
ATOM   1501 O  OG1 . THR   A 1 194 ? -22.046 35.459 26.617 1.000 23.951  ? 193 THR   AAA OG1 1 ? 
ATOM   1502 C  CG2 . THR   A 1 194 ? -21.895 35.514 24.197 1.000 23.455  ? 193 THR   AAA CG2 1 ? 
ATOM   1503 N  N   . TYR   A 1 195 ? -21.072 32.662 27.019 1.000 21.679  ? 194 TYR   AAA N   1 ? 
ATOM   1504 C  CA  . TYR   A 1 195 ? -21.805 31.404 27.310 1.000 21.606  ? 194 TYR   AAA CA  1 ? 
ATOM   1505 C  C   . TYR   A 1 195 ? -22.482 31.579 28.670 1.000 23.242  ? 194 TYR   AAA C   1 ? 
ATOM   1506 O  O   . TYR   A 1 195 ? -22.046 32.370 29.520 1.000 20.435  ? 194 TYR   AAA O   1 ? 
ATOM   1507 C  CB  . TYR   A 1 195 ? -20.857 30.199 27.186 1.000 22.420  ? 194 TYR   AAA CB  1 ? 
ATOM   1508 C  CG  . TYR   A 1 195 ? -19.973 30.028 28.387 1.000 22.311  ? 194 TYR   AAA CG  1 ? 
ATOM   1509 C  CD1 . TYR   A 1 195 ? -18.801 30.754 28.522 1.000 19.494  ? 194 TYR   AAA CD1 1 ? 
ATOM   1510 C  CD2 . TYR   A 1 195 ? -20.362 29.232 29.455 1.000 20.467  ? 194 TYR   AAA CD2 1 ? 
ATOM   1511 C  CE1 . TYR   A 1 195 ? -17.998 30.632 29.643 1.000 20.785  ? 194 TYR   AAA CE1 1 ? 
ATOM   1512 C  CE2 . TYR   A 1 195 ? -19.576 29.117 30.590 1.000 21.616  ? 194 TYR   AAA CE2 1 ? 
ATOM   1513 C  CZ  . TYR   A 1 195 ? -18.411 29.867 30.720 1.000 20.821  ? 194 TYR   AAA CZ  1 ? 
ATOM   1514 O  OH  . TYR   A 1 195 ? -17.618 29.755 31.829 1.000 20.885  ? 194 TYR   AAA OH  1 ? 
ATOM   1515 N  N   . PRO   A 1 196 ? -23.624 30.886 28.865 1.000 23.040  ? 195 PRO   AAA N   1 ? 
ATOM   1516 C  CA  . PRO   A 1 196 ? -24.296 30.862 30.157 1.000 23.149  ? 195 PRO   AAA CA  1 ? 
ATOM   1517 C  C   . PRO   A 1 196 ? -23.559 29.938 31.124 1.000 24.145  ? 195 PRO   AAA C   1 ? 
ATOM   1518 O  O   . PRO   A 1 196 ? -23.321 28.773 30.812 1.000 22.771  ? 195 PRO   AAA O   1 ? 
ATOM   1519 C  CB  . PRO   A 1 196 ? -25.699 30.329 29.826 1.000 24.255  ? 195 PRO   AAA CB  1 ? 
ATOM   1520 C  CG  . PRO   A 1 196 ? -25.472 29.466 28.608 1.000 26.004  ? 195 PRO   AAA CG  1 ? 
ATOM   1521 C  CD  . PRO   A 1 196 ? -24.367 30.156 27.830 1.000 25.635  ? 195 PRO   AAA CD  1 ? 
ATOM   1522 N  N   . GLY   A 1 197 ? -23.271 30.428 32.317 1.000 23.184  ? 196 GLY   AAA N   1 ? 
ATOM   1523 C  CA  . GLY   A 1 197 ? -22.509 29.667 33.308 1.000 22.939  ? 196 GLY   AAA CA  1 ? 
ATOM   1524 C  C   . GLY   A 1 197 ? -22.805 30.115 34.716 1.000 20.413  ? 196 GLY   AAA C   1 ? 
ATOM   1525 O  O   . GLY   A 1 197 ? -23.970 30.462 35.054 1.000 22.991  ? 196 GLY   AAA O   1 ? 
ATOM   1526 N  N   . SER   A 1 198 ? -21.774 30.022 35.544 1.000 21.550  ? 197 SER   AAA N   1 ? 
ATOM   1527 C  CA  . SER   A 1 198 ? -21.920 30.040 37.014 1.000 19.601  ? 197 SER   AAA CA  1 ? 
ATOM   1528 C  C   . SER   A 1 198 ? -20.809 30.882 37.636 1.000 18.280  ? 197 SER   AAA C   1 ? 
ATOM   1529 O  O   . SER   A 1 198 ? -19.797 31.113 36.968 1.000 19.216  ? 197 SER   AAA O   1 ? 
ATOM   1530 C  CB  . SER   A 1 198 ? -21.873 28.646 37.547 1.000 22.320  ? 197 SER   AAA CB  1 ? 
ATOM   1531 O  OG  . SER   A 1 198 ? -20.535 28.158 37.517 1.000 24.178  ? 197 SER   AAA OG  1 ? 
ATOM   1532 N  N   . LEU   A 1 199 ? -20.966 31.173 38.929 1.000 20.620  ? 198 LEU   AAA N   1 ? 
ATOM   1533 C  CA  . LEU   A 1 199 ? -19.823 31.594 39.769 1.000 18.814  ? 198 LEU   AAA CA  1 ? 
ATOM   1534 C  C   . LEU   A 1 199 ? -18.816 30.453 39.785 1.000 18.378  ? 198 LEU   AAA C   1 ? 
ATOM   1535 O  O   . LEU   A 1 199 ? -19.234 29.265 39.756 1.000 19.696  ? 198 LEU   AAA O   1 ? 
ATOM   1536 C  CB  . LEU   A 1 199 ? -20.290 31.898 41.183 1.000 21.265  ? 198 LEU   AAA CB  1 ? 
ATOM   1537 C  CG  . LEU   A 1 199 ? -21.365 32.973 41.291 1.000 20.009  ? 198 LEU   AAA CG  1 ? 
ATOM   1538 C  CD1 . LEU   A 1 199 ? -21.799 33.109 42.730 1.000 22.882  ? 198 LEU   AAA CD1 1 ? 
ATOM   1539 C  CD2 . LEU   A 1 199 ? -20.870 34.295 40.759 1.000 22.706  ? 198 LEU   AAA CD2 1 ? 
ATOM   1540 N  N   . THR   A 1 200 ? -17.537 30.735 39.812 1.000 18.503  ? 199 THR   AAA N   1 ? 
ATOM   1541 C  CA  . THR   A 1 200 ? -16.511 29.664 39.693 1.000 18.599  ? 199 THR   AAA CA  1 ? 
ATOM   1542 C  C   . THR   A 1 200 ? -16.111 29.119 41.074 1.000 18.769  ? 199 THR   AAA C   1 ? 
ATOM   1543 O  O   . THR   A 1 200 ? -15.162 28.327 41.136 1.000 21.717  ? 199 THR   AAA O   1 ? 
ATOM   1544 C  CB  . THR   A 1 200 ? -15.268 30.118 38.912 1.000 21.468  ? 199 THR   AAA CB  1 ? 
ATOM   1545 O  OG1 . THR   A 1 200 ? -14.597 31.165 39.615 1.000 20.109  ? 199 THR   AAA OG1 1 ? 
ATOM   1546 C  CG2 . THR   A 1 200 ? -15.602 30.516 37.490 1.000 22.018  ? 199 THR   AAA CG2 1 ? 
ATOM   1547 N  N   . HIS   A 1 201 ? -16.758 29.583 42.137 1.000 19.336  ? 200 HIS   AAA N   1 ? 
ATOM   1548 C  CA  . HIS   A 1 201 ? -16.545 29.108 43.518 1.000 20.477  ? 200 HIS   AAA CA  1 ? 
ATOM   1549 C  C   . HIS   A 1 201 ? -17.870 29.199 44.246 1.000 19.247  ? 200 HIS   AAA C   1 ? 
ATOM   1550 O  O   . HIS   A 1 201 ? -18.838 29.888 43.809 1.000 21.022  ? 200 HIS   AAA O   1 ? 
ATOM   1551 C  CB  . HIS   A 1 201 ? -15.322 29.755 44.197 1.000 22.306  ? 200 HIS   AAA CB  1 ? 
ATOM   1552 C  CG  . HIS   A 1 201 ? -15.440 31.230 44.445 1.000 20.955  ? 200 HIS   AAA CG  1 ? 
ATOM   1553 N  ND1 . HIS   A 1 201 ? -14.496 32.178 44.038 1.000 25.944  ? 200 HIS   AAA ND1 1 ? 
ATOM   1554 C  CD2 . HIS   A 1 201 ? -16.308 31.857 45.254 1.000 18.588  ? 200 HIS   AAA CD2 1 ? 
ATOM   1555 C  CE1 . HIS   A 1 201 ? -14.875 33.389 44.518 1.000 21.903  ? 200 HIS   AAA CE1 1 ? 
ATOM   1556 N  NE2 . HIS   A 1 201 ? -15.976 33.226 45.284 1.000 25.566  ? 200 HIS   AAA NE2 1 ? 
ATOM   1557 N  N   . PRO   A 1 202 ? -17.958 28.534 45.406 1.000 20.580  ? 201 PRO   AAA N   1 ? 
ATOM   1558 C  CA  . PRO   A 1 202 ? -19.185 28.568 46.186 1.000 21.377  ? 201 PRO   AAA CA  1 ? 
ATOM   1559 C  C   . PRO   A 1 202 ? -19.609 30.005 46.402 1.000 22.118  ? 201 PRO   AAA C   1 ? 
ATOM   1560 O  O   . PRO   A 1 202 ? -18.791 30.896 46.698 1.000 22.718  ? 201 PRO   AAA O   1 ? 
ATOM   1561 C  CB  . PRO   A 1 202 ? -18.807 27.800 47.466 1.000 21.637  ? 201 PRO   AAA CB  1 ? 
ATOM   1562 C  CG  . PRO   A 1 202 ? -17.807 26.818 46.944 1.000 23.329  ? 201 PRO   AAA CG  1 ? 
ATOM   1563 C  CD  . PRO   A 1 202 ? -16.960 27.627 45.992 1.000 23.005  ? 201 PRO   AAA CD  1 ? 
ATOM   1564 N  N   . PRO   A 1 203 ? -20.912 30.249 46.288 1.000 20.641  ? 202 PRO   AAA N   1 ? 
ATOM   1565 C  CA  . PRO   A 1 203 ? -21.953 29.212 46.142 1.000 22.431  ? 202 PRO   AAA CA  1 ? 
ATOM   1566 C  C   . PRO   A 1 203 ? -22.306 28.702 44.727 1.000 20.847  ? 202 PRO   AAA C   1 ? 
ATOM   1567 O  O   . PRO   A 1 203 ? -23.338 28.015 44.576 1.000 23.190  ? 202 PRO   AAA O   1 ? 
ATOM   1568 C  CB  . PRO   A 1 203 ? -23.191 29.941 46.718 1.000 23.473  ? 202 PRO   AAA CB  1 ? 
ATOM   1569 C  CG  . PRO   A 1 203 ? -22.944 31.378 46.382 1.000 23.474  ? 202 PRO   AAA CG  1 ? 
ATOM   1570 C  CD  . PRO   A 1 203 ? -21.458 31.581 46.525 1.000 23.200  ? 202 PRO   AAA CD  1 ? 
ATOM   1571 N  N   . LEU   A 1 204 ? -21.474 28.976 43.730 1.000 21.470  ? 203 LEU   AAA N   1 ? 
ATOM   1572 C  CA  . LEU   A 1 204 ? -21.529 28.346 42.383 1.000 22.416  ? 203 LEU   AAA CA  1 ? 
ATOM   1573 C  C   . LEU   A 1 204 ? -22.881 28.554 41.676 1.000 23.430  ? 203 LEU   AAA C   1 ? 
ATOM   1574 O  O   . LEU   A 1 204 ? -23.202 27.777 40.721 1.000 22.700  ? 203 LEU   AAA O   1 ? 
ATOM   1575 C  CB  . LEU   A 1 204 ? -21.257 26.840 42.534 1.000 22.104  ? 203 LEU   AAA CB  1 ? 
ATOM   1576 C  CG  . LEU   A 1 204 ? -19.854 26.506 43.023 1.000 26.406  ? 203 LEU   AAA CG  1 ? 
ATOM   1577 C  CD1 . LEU   A 1 204 ? -19.840 25.039 43.483 1.000 27.608  ? 203 LEU   AAA CD1 1 ? 
ATOM   1578 C  CD2 . LEU   A 1 204 ? -18.804 26.670 41.936 1.000 25.147  ? 203 LEU   AAA CD2 1 ? 
ATOM   1579 N  N   . TYR   A 1 205 ? -23.616 29.615 41.997 1.000 22.872  ? 204 TYR   AAA N   1 ? 
ATOM   1580 C  CA  . TYR   A 1 205 ? -24.922 29.894 41.355 1.000 21.103  ? 204 TYR   AAA CA  1 ? 
ATOM   1581 C  C   . TYR   A 1 205 ? -24.765 29.927 39.829 1.000 20.371  ? 204 TYR   AAA C   1 ? 
ATOM   1582 O  O   . TYR   A 1 205 ? -23.766 30.547 39.316 1.000 20.783  ? 204 TYR   AAA O   1 ? 
ATOM   1583 C  CB  . TYR   A 1 205 ? -25.430 31.298 41.731 1.000 20.868  ? 204 TYR   AAA CB  1 ? 
ATOM   1584 C  CG  . TYR   A 1 205 ? -25.904 31.492 43.144 1.000 23.663  ? 204 TYR   AAA CG  1 ? 
ATOM   1585 C  CD1 . TYR   A 1 205 ? -26.777 30.605 43.758 1.000 29.885  ? 204 TYR   AAA CD1 1 ? 
ATOM   1586 C  CD2 . TYR   A 1 205 ? -25.559 32.626 43.847 1.000 24.070  ? 204 TYR   AAA CD2 1 ? 
ATOM   1587 C  CE1 . TYR   A 1 205 ? -27.248 30.834 45.046 1.000 37.496  ? 204 TYR   AAA CE1 1 ? 
ATOM   1588 C  CE2 . TYR   A 1 205 ? -25.988 32.845 45.140 1.000 24.398  ? 204 TYR   AAA CE2 1 ? 
ATOM   1589 C  CZ  . TYR   A 1 205 ? -26.869 31.977 45.734 1.000 32.663  ? 204 TYR   AAA CZ  1 ? 
ATOM   1590 O  OH  . TYR   A 1 205 ? -27.307 32.232 47.007 1.000 45.613  ? 204 TYR   AAA OH  1 ? 
ATOM   1591 N  N   . GLU   A 1 206 ? -25.762 29.385 39.116 1.000 22.667  ? 205 GLU   AAA N   1 ? 
ATOM   1592 C  CA  . GLU   A 1 206 ? -25.778 29.339 37.633 1.000 23.060  ? 205 GLU   AAA CA  1 ? 
ATOM   1593 C  C   . GLU   A 1 206 ? -26.474 30.617 37.148 1.000 20.343  ? 205 GLU   AAA C   1 ? 
ATOM   1594 O  O   . GLU   A 1 206 ? -27.493 30.543 36.465 1.000 22.970  ? 205 GLU   AAA O   1 ? 
ATOM   1595 C  CB  . GLU   A 1 206 ? -26.405 28.010 37.189 1.000 26.091  ? 205 GLU   AAA CB  1 ? 
ATOM   1596 C  CG  . GLU   A 1 206 ? -25.502 26.827 37.559 1.000 27.348  ? 205 GLU   AAA CG  1 ? 
ATOM   1597 C  CD  . GLU   A 1 206 ? -25.881 25.461 37.018 1.000 27.620  ? 205 GLU   AAA CD  1 ? 
ATOM   1598 O  OE1 . GLU   A 1 206 ? -24.969 24.595 36.997 1.000 29.027  ? 205 GLU   AAA OE1 1 ? 
ATOM   1599 O  OE2 . GLU   A 1 206 ? -27.073 25.267 36.658 1.000 30.177  ? 205 GLU   AAA OE2 1 ? 
ATOM   1600 N  N   . SER   A 1 207 ? -25.890 31.775 37.491 1.000 20.866  ? 206 SER   AAA N   1 ? 
ATOM   1601 C  CA  . SER   A 1 207 ? -26.518 33.104 37.385 1.000 21.808  ? 206 SER   AAA CA  1 ? 
ATOM   1602 C  C   . SER   A 1 207 ? -25.667 33.975 36.460 1.000 21.135  ? 206 SER   AAA C   1 ? 
ATOM   1603 O  O   . SER   A 1 207 ? -26.024 35.187 36.286 1.000 22.968  ? 206 SER   AAA O   1 ? 
ATOM   1604 C  CB  . SER   A 1 207 ? -26.636 33.647 38.750 1.000 22.704  ? 206 SER   AAA CB  1 ? 
ATOM   1605 O  OG  . SER   A 1 207 ? -25.343 33.777 39.329 1.000 23.812  ? 206 SER   AAA OG  1 ? 
ATOM   1606 N  N   . VAL   A 1 208 ? -24.564 33.462 35.900 1.000 18.735  ? 207 VAL   AAA N   1 ? 
ATOM   1607 C  CA  . VAL   A 1 208 ? -23.541 34.294 35.201 1.000 18.643  ? 207 VAL   AAA CA  1 ? 
ATOM   1608 C  C   . VAL   A 1 208 ? -23.636 34.127 33.685 1.000 21.618  ? 207 VAL   AAA C   1 ? 
ATOM   1609 O  O   . VAL   A 1 208 ? -23.446 33.015 33.173 1.000 25.493  ? 207 VAL   AAA O   1 ? 
ATOM   1610 C  CB  . VAL   A 1 208 ? -22.106 34.015 35.688 1.000 18.240  ? 207 VAL   AAA CB  1 ? 
ATOM   1611 C  CG1 . VAL   A 1 208 ? -21.086 34.885 34.985 1.000 19.824  ? 207 VAL   AAA CG1 1 ? 
ATOM   1612 C  CG2 . VAL   A 1 208 ? -21.989 34.195 37.189 1.000 18.806  ? 207 VAL   AAA CG2 1 ? 
ATOM   1613 N  N   . THR   A 1 209 ? -23.791 35.250 32.987 1.000 22.534  ? 208 THR   AAA N   1 ? 
ATOM   1614 C  CA  . THR   A 1 209 ? -23.448 35.401 31.561 1.000 19.852  ? 208 THR   AAA CA  1 ? 
ATOM   1615 C  C   . THR   A 1 209 ? -21.983 35.826 31.482 1.000 21.142  ? 208 THR   AAA C   1 ? 
ATOM   1616 O  O   . THR   A 1 209 ? -21.626 36.964 31.882 1.000 21.433  ? 208 THR   AAA O   1 ? 
ATOM   1617 C  CB  . THR   A 1 209 ? -24.372 36.377 30.831 1.000 24.333  ? 208 THR   AAA CB  1 ? 
ATOM   1618 O  OG1 . THR   A 1 209 ? -25.710 35.962 31.090 1.000 27.362  ? 208 THR   AAA OG1 1 ? 
ATOM   1619 C  CG2 . THR   A 1 209 ? -24.103 36.409 29.345 1.000 29.735  ? 208 THR   AAA CG2 1 ? 
ATOM   1620 N  N   . TRP   A 1 210 ? -21.164 34.946 30.959 1.000 19.600  ? 209 TRP   AAA N   1 ? 
ATOM   1621 C  CA  . TRP   A 1 210 ? -19.701 35.121 30.836 1.000 20.363  ? 209 TRP   AAA CA  1 ? 
ATOM   1622 C  C   . TRP   A 1 210 ? -19.391 35.834 29.535 1.000 19.209  ? 209 TRP   AAA C   1 ? 
ATOM   1623 O  O   . TRP   A 1 210 ? -20.013 35.557 28.523 1.000 21.765  ? 209 TRP   AAA O   1 ? 
ATOM   1624 C  CB  . TRP   A 1 210 ? -18.963 33.777 30.915 1.000 19.982  ? 209 TRP   AAA CB  1 ? 
ATOM   1625 C  CG  . TRP   A 1 210 ? -18.789 33.341 32.330 1.000 19.282  ? 209 TRP   AAA CG  1 ? 
ATOM   1626 C  CD1 . TRP   A 1 210 ? -19.569 32.465 33.031 1.000 21.070  ? 209 TRP   AAA CD1 1 ? 
ATOM   1627 C  CD2 . TRP   A 1 210 ? -17.792 33.794 33.243 1.000 17.182  ? 209 TRP   AAA CD2 1 ? 
ATOM   1628 N  NE1 . TRP   A 1 210 ? -19.139 32.369 34.321 1.000 19.973  ? 209 TRP   AAA NE1 1 ? 
ATOM   1629 C  CE2 . TRP   A 1 210 ? -18.049 33.184 34.481 1.000 18.232  ? 209 TRP   AAA CE2 1 ? 
ATOM   1630 C  CE3 . TRP   A 1 210 ? -16.725 34.702 33.149 1.000 16.840  ? 209 TRP   AAA CE3 1 ? 
ATOM   1631 C  CZ2 . TRP   A 1 210 ? -17.274 33.436 35.608 1.000 19.002  ? 209 TRP   AAA CZ2 1 ? 
ATOM   1632 C  CZ3 . TRP   A 1 210 ? -15.940 34.896 34.246 1.000 17.546  ? 209 TRP   AAA CZ3 1 ? 
ATOM   1633 C  CH2 . TRP   A 1 210 ? -16.214 34.289 35.467 1.000 18.865  ? 209 TRP   AAA CH2 1 ? 
ATOM   1634 N  N   . ILE   A 1 211 ? -18.516 36.832 29.651 1.000 20.210  ? 210 ILE   AAA N   1 ? 
ATOM   1635 C  CA  . ILE   A 1 211 ? -17.915 37.541 28.503 1.000 18.869  ? 210 ILE   AAA CA  1 ? 
ATOM   1636 C  C   . ILE   A 1 211 ? -16.421 37.306 28.584 1.000 18.088  ? 210 ILE   AAA C   1 ? 
ATOM   1637 O  O   . ILE   A 1 211 ? -15.830 37.758 29.532 1.000 20.671  ? 210 ILE   AAA O   1 ? 
ATOM   1638 C  CB  . ILE   A 1 211 ? -18.223 39.055 28.566 1.000 18.609  ? 210 ILE   AAA CB  1 ? 
ATOM   1639 C  CG1 . ILE   A 1 211 ? -19.721 39.345 28.666 1.000 19.861  ? 210 ILE   AAA CG1 1 ? 
ATOM   1640 C  CG2 . ILE   A 1 211 ? -17.580 39.761 27.384 1.000 22.382  ? 210 ILE   AAA CG2 1 ? 
ATOM   1641 C  CD1 . ILE   A 1 211 ? -20.546 38.970 27.476 1.000 24.076  ? 210 ILE   AAA CD1 1 ? 
ATOM   1642 N  N   . ILE   A 1 212 ? -15.899 36.421 27.743 1.000 21.116  ? 211 ILE   AAA N   1 ? 
ATOM   1643 C  CA  . ILE   A 1 212 ? -14.461 36.099 27.756 1.000 19.170  ? 211 ILE   AAA CA  1 ? 
ATOM   1644 C  C   . ILE   A 1 212 ? -13.801 36.823 26.600 1.000 19.606  ? 211 ILE   AAA C   1 ? 
ATOM   1645 O  O   . ILE   A 1 212 ? -14.194 36.612 25.460 1.000 19.710  ? 211 ILE   AAA O   1 ? 
ATOM   1646 C  CB  . ILE   A 1 212 ? -14.225 34.585 27.669 1.000 18.908  ? 211 ILE   AAA CB  1 ? 
ATOM   1647 C  CG1 . ILE   A 1 212 ? -15.018 33.800 28.720 1.000 22.877  ? 211 ILE   AAA CG1 1 ? 
ATOM   1648 C  CG2 . ILE   A 1 212 ? -12.738 34.360 27.750 1.000 21.738  ? 211 ILE   AAA CG2 1 ? 
ATOM   1649 C  CD1 . ILE   A 1 212 ? -14.661 34.135 30.167 1.000 22.124  ? 211 ILE   AAA CD1 1 ? 
ATOM   1650 N  N   . CYS   A 1 213 ? -12.815 37.647 26.924 1.000 20.316  ? 212 CYS   AAA N   1 ? 
ATOM   1651 C  CA  . CYS   A 1 213 ? -12.061 38.434 25.925 1.000 22.012  ? 212 CYS   AAA CA  1 ? 
ATOM   1652 C  C   . CYS   A 1 213 ? -11.185 37.492 25.100 1.000 21.000  ? 212 CYS   AAA C   1 ? 
ATOM   1653 O  O   . CYS   A 1 213 ? -10.564 36.575 25.675 1.000 21.059  ? 212 CYS   AAA O   1 ? 
ATOM   1654 C  CB  . CYS   A 1 213 ? -11.254 39.535 26.593 1.000 20.167  ? 212 CYS   AAA CB  1 ? 
ATOM   1655 S  SG  . CYS   A 1 213 ? -12.309 40.852 27.257 1.000 24.948  ? 212 CYS   AAA SG  1 ? 
ATOM   1656 N  N   . LYS   A 1 214 ? -11.154 37.714 23.795 1.000 20.637  ? 213 LYS   AAA N   1 ? 
ATOM   1657 C  CA  . LYS   A 1 214 ? -10.254 37.010 22.856 1.000 22.489  ? 213 LYS   AAA CA  1 ? 
ATOM   1658 C  C   . LYS   A 1 214 ? -8.790  37.395 23.124 1.000 20.355  ? 213 LYS   AAA C   1 ? 
ATOM   1659 O  O   . LYS   A 1 214 ? -7.883  36.512 23.051 1.000 22.296  ? 213 LYS   AAA O   1 ? 
ATOM   1660 C  CB  . LYS   A 1 214 ? -10.697 37.408 21.440 1.000 27.266  ? 213 LYS   AAA CB  1 ? 
ATOM   1661 C  CG  . LYS   A 1 214 ? -9.958  36.726 20.307 1.000 34.870  ? 213 LYS   AAA CG  1 ? 
ATOM   1662 C  CD  . LYS   A 1 214 ? -10.114 37.432 18.981 1.000 34.186  ? 213 LYS   AAA CD  1 ? 
ATOM   1663 C  CE  . LYS   A 1 214 ? -9.332  38.724 18.942 1.000 34.536  ? 213 LYS   AAA CE  1 ? 
ATOM   1664 N  NZ  . LYS   A 1 214 ? -9.466  39.345 17.614 1.000 40.156  ? 213 LYS   AAA NZ  1 ? 
ATOM   1665 N  N   . GLU   A 1 215 ? -8.528  38.717 23.277 1.000 19.827  ? 214 GLU   AAA N   1 ? 
ATOM   1666 C  CA  . GLU   A 1 215 ? -7.154  39.228 23.526 1.000 20.218  ? 214 GLU   AAA CA  1 ? 
ATOM   1667 C  C   . GLU   A 1 215 ? -6.797  39.012 25.000 1.000 18.508  ? 214 GLU   AAA C   1 ? 
ATOM   1668 O  O   . GLU   A 1 215 ? -7.626  39.347 25.901 1.000 18.680  ? 214 GLU   AAA O   1 ? 
ATOM   1669 C  CB  . GLU   A 1 215 ? -7.010  40.725 23.236 1.000 25.183  ? 214 GLU   AAA CB  1 ? 
ATOM   1670 C  CG  . GLU   A 1 215 ? -6.604  41.045 21.824 1.000 33.523  ? 214 GLU   AAA CG  1 ? 
ATOM   1671 C  CD  . GLU   A 1 215 ? -6.392  42.527 21.553 1.000 30.109  ? 214 GLU   AAA CD  1 ? 
ATOM   1672 O  OE1 . GLU   A 1 215 ? -6.435  43.304 22.528 1.000 31.128  ? 214 GLU   AAA OE1 1 ? 
ATOM   1673 O  OE2 . GLU   A 1 215 ? -6.192  42.876 20.369 1.000 43.501  ? 214 GLU   AAA OE2 1 ? 
ATOM   1674 N  N   . SER   A 1 216 ? -5.598  38.487 25.255 1.000 19.073  ? 215 SER   AAA N   1 ? 
ATOM   1675 C  CA  . SER   A 1 216 ? -5.042  38.408 26.627 1.000 20.489  ? 215 SER   AAA CA  1 ? 
ATOM   1676 C  C   . SER   A 1 216 ? -4.505  39.789 27.056 1.000 19.050  ? 215 SER   AAA C   1 ? 
ATOM   1677 O  O   . SER   A 1 216 ? -4.330  40.670 26.181 1.000 22.428  ? 215 SER   AAA O   1 ? 
ATOM   1678 C  CB  . SER   A 1 216 ? -3.957  37.361 26.713 1.000 19.226  ? 215 SER   AAA CB  1 ? 
ATOM   1679 O  OG  . SER   A 1 216 ? -2.857  37.702 25.887 1.000 20.804  ? 215 SER   AAA OG  1 ? 
ATOM   1680 N  N   . ILE   A 1 217 ? -4.233  39.934 28.343 1.000 18.970  ? 216 ILE   AAA N   1 ? 
ATOM   1681 C  CA  . ILE   A 1 217 ? -3.367  41.008 28.888 1.000 21.481  ? 216 ILE   AAA CA  1 ? 
ATOM   1682 C  C   . ILE   A 1 217 ? -2.141  40.361 29.503 1.000 22.122  ? 216 ILE   AAA C   1 ? 
ATOM   1683 O  O   . ILE   A 1 217 ? -2.172  39.124 29.819 1.000 23.445  ? 216 ILE   AAA O   1 ? 
ATOM   1684 C  CB  . ILE   A 1 217 ? -4.106  41.903 29.897 1.000 20.481  ? 216 ILE   AAA CB  1 ? 
ATOM   1685 C  CG1 . ILE   A 1 217 ? -4.504  41.163 31.175 1.000 20.613  ? 216 ILE   AAA CG1 1 ? 
ATOM   1686 C  CG2 . ILE   A 1 217 ? -5.275  42.595 29.215 1.000 20.956  ? 216 ILE   AAA CG2 1 ? 
ATOM   1687 C  CD1 . ILE   A 1 217 ? -5.155  42.035 32.188 1.000 20.626  ? 216 ILE   AAA CD1 1 ? 
ATOM   1688 N  N   . SER   A 1 218 ? -1.100  41.157 29.660 1.000 18.978  ? 217 SER   AAA N   1 ? 
ATOM   1689 C  CA  A SER   A 1 218 ? 0.182   40.659 30.216 0.500 20.327  ? 217 SER   AAA CA  1 ? 
ATOM   1690 C  CA  B SER   A 1 218 ? 0.199   40.714 30.213 0.500 21.265  ? 217 SER   AAA CA  1 ? 
ATOM   1691 C  C   . SER   A 1 218 ? 0.198   40.715 31.747 1.000 19.926  ? 217 SER   AAA C   1 ? 
ATOM   1692 O  O   . SER   A 1 218 ? -0.619  41.421 32.384 1.000 21.421  ? 217 SER   AAA O   1 ? 
ATOM   1693 C  CB  A SER   A 1 218 ? 1.390   41.343 29.633 0.500 21.169  ? 217 SER   AAA CB  1 ? 
ATOM   1694 C  CB  B SER   A 1 218 ? 1.312   41.557 29.675 0.500 24.423  ? 217 SER   AAA CB  1 ? 
ATOM   1695 O  OG  A SER   A 1 218 ? 1.612   42.617 30.226 0.500 21.485  ? 217 SER   AAA OG  1 ? 
ATOM   1696 O  OG  B SER   A 1 218 ? 2.496   40.793 29.567 0.500 23.989  ? 217 SER   AAA OG  1 ? 
ATOM   1697 N  N   . VAL   A 1 219 ? 1.110   39.940 32.304 1.000 20.204  ? 218 VAL   AAA N   1 ? 
ATOM   1698 C  CA  . VAL   A 1 219 ? 1.463   39.948 33.738 1.000 19.335  ? 218 VAL   AAA CA  1 ? 
ATOM   1699 C  C   . VAL   A 1 219 ? 2.863   39.356 33.818 1.000 22.837  ? 218 VAL   AAA C   1 ? 
ATOM   1700 O  O   . VAL   A 1 219 ? 3.159   38.472 33.009 1.000 23.449  ? 218 VAL   AAA O   1 ? 
ATOM   1701 C  CB  . VAL   A 1 219 ? 0.450   39.184 34.589 1.000 21.501  ? 218 VAL   AAA CB  1 ? 
ATOM   1702 C  CG1 . VAL   A 1 219 ? 0.395   37.718 34.194 1.000 22.465  ? 218 VAL   AAA CG1 1 ? 
ATOM   1703 C  CG2 . VAL   A 1 219 ? 0.750   39.333 36.065 1.000 23.187  ? 218 VAL   AAA CG2 1 ? 
ATOM   1704 N  N   . SER   A 1 220 ? 3.743   39.914 34.648 1.000 22.244  ? 219 SER   AAA N   1 ? 
ATOM   1705 C  CA  . SER   A 1 220 ? 5.111   39.363 34.786 1.000 24.403  ? 219 SER   AAA CA  1 ? 
ATOM   1706 C  C   . SER   A 1 220 ? 5.098   38.218 35.809 1.000 19.412  ? 219 SER   AAA C   1 ? 
ATOM   1707 O  O   . SER   A 1 220 ? 4.188   38.166 36.656 1.000 20.759  ? 219 SER   AAA O   1 ? 
ATOM   1708 C  CB  . SER   A 1 220 ? 6.094   40.442 35.161 1.000 23.993  ? 219 SER   AAA CB  1 ? 
ATOM   1709 O  OG  . SER   A 1 220 ? 5.902   40.828 36.499 1.000 23.483  ? 219 SER   AAA OG  1 ? 
ATOM   1710 N  N   . SER   A 1 221 ? 6.128   37.374 35.769 1.000 25.241  ? 220 SER   AAA N   1 ? 
ATOM   1711 C  CA  A SER   A 1 221 ? 6.397   36.318 36.783 0.500 25.055  ? 220 SER   AAA CA  1 ? 
ATOM   1712 C  CA  B SER   A 1 221 ? 6.341   36.304 36.782 0.500 26.204  ? 220 SER   AAA CA  1 ? 
ATOM   1713 C  C   . SER   A 1 221 ? 6.411   36.932 38.187 1.000 22.076  ? 220 SER   AAA C   1 ? 
ATOM   1714 O  O   . SER   A 1 221 ? 5.892   36.314 39.131 1.000 24.150  ? 220 SER   AAA O   1 ? 
ATOM   1715 C  CB  A SER   A 1 221 ? 7.701   35.640 36.482 0.500 24.658  ? 220 SER   AAA CB  1 ? 
ATOM   1716 C  CB  B SER   A 1 221 ? 7.562   35.477 36.452 0.500 28.551  ? 220 SER   AAA CB  1 ? 
ATOM   1717 O  OG  A SER   A 1 221 ? 7.679   35.071 35.186 0.500 21.965  ? 220 SER   AAA OG  1 ? 
ATOM   1718 O  OG  B SER   A 1 221 ? 7.520   34.213 37.107 0.500 30.762  ? 220 SER   AAA OG  1 ? 
ATOM   1719 N  N   . GLU   A 1 222 ? 6.969   38.147 38.322 1.000 25.754  ? 221 GLU   AAA N   1 ? 
ATOM   1720 C  CA  . GLU   A 1 222 ? 7.117   38.798 39.650 1.000 24.520  ? 221 GLU   AAA CA  1 ? 
ATOM   1721 C  C   . GLU   A 1 222 ? 5.775   39.417 40.096 1.000 24.456  ? 221 GLU   AAA C   1 ? 
ATOM   1722 O  O   . GLU   A 1 222 ? 5.486   39.420 41.290 1.000 26.580  ? 221 GLU   AAA O   1 ? 
ATOM   1723 C  CB  . GLU   A 1 222 ? 8.214   39.869 39.610 1.000 25.539  ? 221 GLU   AAA CB  1 ? 
ATOM   1724 C  CG  . GLU   A 1 222 ? 9.589   39.328 39.274 1.000 23.608  ? 221 GLU   AAA CG  1 ? 
ATOM   1725 C  CD  . GLU   A 1 222 ? 9.821   38.888 37.833 1.000 26.886  ? 221 GLU   AAA CD  1 ? 
ATOM   1726 O  OE1 . GLU   A 1 222 ? 9.311   39.540 36.887 1.000 27.621  ? 221 GLU   AAA OE1 1 ? 
ATOM   1727 O  OE2 . GLU   A 1 222 ? 10.541  37.882 37.654 1.000 35.863  ? 221 GLU   AAA OE2 1 ? 
ATOM   1728 N  N   . GLN   A 1 223 ? 4.955   39.903 39.175 1.000 24.360  ? 222 GLN   AAA N   1 ? 
ATOM   1729 C  CA  . GLN   A 1 223 ? 3.588   40.354 39.524 1.000 22.202  ? 222 GLN   AAA CA  1 ? 
ATOM   1730 C  C   . GLN   A 1 223 ? 2.779   39.138 40.045 1.000 22.388  ? 222 GLN   AAA C   1 ? 
ATOM   1731 O  O   . GLN   A 1 223 ? 2.099   39.245 41.089 1.000 22.591  ? 222 GLN   AAA O   1 ? 
ATOM   1732 C  CB  . GLN   A 1 223 ? 3.003   41.102 38.327 1.000 24.222  ? 222 GLN   AAA CB  1 ? 
ATOM   1733 C  CG  . GLN   A 1 223 ? 3.618   42.492 38.108 1.000 23.669  ? 222 GLN   AAA CG  1 ? 
ATOM   1734 C  CD  . GLN   A 1 223 ? 2.975   43.194 36.948 1.000 23.238  ? 222 GLN   AAA CD  1 ? 
ATOM   1735 O  OE1 . GLN   A 1 223 ? 2.665   42.591 35.912 1.000 21.537  ? 222 GLN   AAA OE1 1 ? 
ATOM   1736 N  NE2 . GLN   A 1 223 ? 2.737   44.485 37.123 1.000 27.697  ? 222 GLN   AAA NE2 1 ? 
ATOM   1737 N  N   . LEU   A 1 224 ? 2.897   37.984 39.400 1.000 24.762  ? 223 LEU   AAA N   1 ? 
ATOM   1738 C  CA  . LEU   A 1 224 ? 2.160   36.781 39.879 1.000 24.563  ? 223 LEU   AAA CA  1 ? 
ATOM   1739 C  C   . LEU   A 1 224 ? 2.683   36.415 41.274 1.000 24.495  ? 223 LEU   AAA C   1 ? 
ATOM   1740 O  O   . LEU   A 1 224 ? 1.858   36.019 42.131 1.000 23.511  ? 223 LEU   AAA O   1 ? 
ATOM   1741 C  CB  . LEU   A 1 224 ? 2.366   35.630 38.897 1.000 26.041  ? 223 LEU   AAA CB  1 ? 
ATOM   1742 C  CG  . LEU   A 1 224 ? 1.658   35.812 37.561 1.000 24.472  ? 223 LEU   AAA CG  1 ? 
ATOM   1743 C  CD1 . LEU   A 1 224 ? 2.224   34.887 36.509 1.000 29.173  ? 223 LEU   AAA CD1 1 ? 
ATOM   1744 C  CD2 . LEU   A 1 224 ? 0.167   35.611 37.691 1.000 27.148  ? 223 LEU   AAA CD2 1 ? 
ATOM   1745 N  N   . ALA   A 1 225 ? 4.006   36.502 41.504 1.000 24.085  ? 224 ALA   AAA N   1 ? 
ATOM   1746 C  CA  . ALA   A 1 225 ? 4.601   36.242 42.838 1.000 24.664  ? 224 ALA   AAA CA  1 ? 
ATOM   1747 C  C   . ALA   A 1 225 ? 3.917   37.127 43.899 1.000 22.549  ? 224 ALA   AAA C   1 ? 
ATOM   1748 O  O   . ALA   A 1 225 ? 3.722   36.658 45.025 1.000 23.272  ? 224 ALA   AAA O   1 ? 
ATOM   1749 C  CB  . ALA   A 1 225 ? 6.087   36.472 42.827 1.000 27.189  ? 224 ALA   AAA CB  1 ? 
ATOM   1750 N  N   . GLN   A 1 226 ? 3.576   38.384 43.577 1.000 23.294  ? 225 GLN   AAA N   1 ? 
ATOM   1751 C  CA  . GLN   A 1 226 ? 2.906   39.285 44.555 1.000 22.416  ? 225 GLN   AAA CA  1 ? 
ATOM   1752 C  C   . GLN   A 1 226 ? 1.545   38.692 44.946 1.000 19.747  ? 225 GLN   AAA C   1 ? 
ATOM   1753 O  O   . GLN   A 1 226 ? 1.220   38.701 46.142 1.000 23.824  ? 225 GLN   AAA O   1 ? 
ATOM   1754 C  CB  . GLN   A 1 226 ? 2.759   40.708 44.013 1.000 21.385  ? 225 GLN   AAA CB  1 ? 
ATOM   1755 C  CG  . GLN   A 1 226 ? 4.080   41.451 43.958 1.000 23.334  ? 225 GLN   AAA CG  1 ? 
ATOM   1756 C  CD  . GLN   A 1 226 ? 3.893   42.897 43.595 1.000 24.882  ? 225 GLN   AAA CD  1 ? 
ATOM   1757 O  OE1 . GLN   A 1 226 ? 4.199   43.317 42.473 1.000 25.469  ? 225 GLN   AAA OE1 1 ? 
ATOM   1758 N  NE2 . GLN   A 1 226 ? 3.403   43.651 44.576 1.000 25.076  ? 225 GLN   AAA NE2 1 ? 
ATOM   1759 N  N   . PHE   A 1 227 ? 0.748   38.215 43.987 1.000 19.324  ? 226 PHE   AAA N   1 ? 
ATOM   1760 C  CA  . PHE   A 1 227 ? -0.535  37.547 44.310 1.000 19.505  ? 226 PHE   AAA CA  1 ? 
ATOM   1761 C  C   . PHE   A 1 227 ? -0.238  36.380 45.260 1.000 19.541  ? 226 PHE   AAA C   1 ? 
ATOM   1762 O  O   . PHE   A 1 227 ? -0.899  36.277 46.291 1.000 21.950  ? 226 PHE   AAA O   1 ? 
ATOM   1763 C  CB  . PHE   A 1 227 ? -1.255  37.033 43.072 1.000 20.674  ? 226 PHE   AAA CB  1 ? 
ATOM   1764 C  CG  . PHE   A 1 227 ? -1.756  38.022 42.065 1.000 23.482  ? 226 PHE   AAA CG  1 ? 
ATOM   1765 C  CD1 . PHE   A 1 227 ? -2.046  39.336 42.416 1.000 27.658  ? 226 PHE   AAA CD1 1 ? 
ATOM   1766 C  CD2 . PHE   A 1 227 ? -1.952  37.638 40.757 1.000 25.097  ? 226 PHE   AAA CD2 1 ? 
ATOM   1767 C  CE1 . PHE   A 1 227 ? -2.530  40.222 41.472 1.000 30.565  ? 226 PHE   AAA CE1 1 ? 
ATOM   1768 C  CE2 . PHE   A 1 227 ? -2.447  38.527 39.821 1.000 27.129  ? 226 PHE   AAA CE2 1 ? 
ATOM   1769 C  CZ  . PHE   A 1 227 ? -2.757  39.813 40.184 1.000 27.404  ? 226 PHE   AAA CZ  1 ? 
ATOM   1770 N  N   . ARG   A 1 228 ? 0.750   35.549 44.932 1.000 21.603  ? 227 ARG   AAA N   1 ? 
ATOM   1771 C  CA  . ARG   A 1 228 ? 0.977   34.260 45.674 1.000 21.625  ? 227 ARG   AAA CA  1 ? 
ATOM   1772 C  C   . ARG   A 1 228 ? 1.570   34.556 47.056 1.000 21.763  ? 227 ARG   AAA C   1 ? 
ATOM   1773 O  O   . ARG   A 1 228 ? 1.520   33.694 47.934 1.000 24.615  ? 227 ARG   AAA O   1 ? 
ATOM   1774 C  CB  . ARG   A 1 228 ? 1.925   33.332 44.912 1.000 24.628  ? 227 ARG   AAA CB  1 ? 
ATOM   1775 C  CG  . ARG   A 1 228 ? 1.470   32.978 43.511 1.000 25.952  ? 227 ARG   AAA CG  1 ? 
ATOM   1776 C  CD  . ARG   A 1 228 ? 2.192   31.772 42.949 1.000 31.310  ? 227 ARG   AAA CD  1 ? 
ATOM   1777 N  NE  . ARG   A 1 228 ? 2.044   31.718 41.502 1.000 30.995  ? 227 ARG   AAA NE  1 ? 
ATOM   1778 C  CZ  . ARG   A 1 228 ? 2.982   32.023 40.617 1.000 30.397  ? 227 ARG   AAA CZ  1 ? 
ATOM   1779 N  NH1 . ARG   A 1 228 ? 2.704   31.951 39.323 1.000 37.206  ? 227 ARG   AAA NH1 1 ? 
ATOM   1780 N  NH2 . ARG   A 1 228 ? 4.190   32.388 41.014 1.000 36.139  ? 227 ARG   AAA NH2 1 ? 
ATOM   1781 N  N   . SER   A 1 229 ? 2.067   35.787 47.282 1.000 21.039  ? 228 SER   AAA N   1 ? 
ATOM   1782 C  CA  . SER   A 1 229 ? 2.653   36.139 48.593 1.000 21.634  ? 228 SER   AAA CA  1 ? 
ATOM   1783 C  C   . SER   A 1 229 ? 1.542   36.640 49.526 1.000 22.500  ? 228 SER   AAA C   1 ? 
ATOM   1784 O  O   . SER   A 1 229 ? 1.816   36.796 50.740 1.000 23.471  ? 228 SER   AAA O   1 ? 
ATOM   1785 C  CB  . SER   A 1 229 ? 3.787   37.105 48.443 1.000 29.412  ? 228 SER   AAA CB  1 ? 
ATOM   1786 O  OG  . SER   A 1 229 ? 3.315   38.350 47.980 1.000 36.146  ? 228 SER   AAA OG  1 ? 
ATOM   1787 N  N   . LEU   A 1 230 ? 0.317   36.859 49.020 1.000 22.158  ? 229 LEU   AAA N   1 ? 
ATOM   1788 C  CA  . LEU   A 1 230 ? -0.802  37.186 49.945 1.000 22.541  ? 229 LEU   AAA CA  1 ? 
ATOM   1789 C  C   . LEU   A 1 230 ? -1.013  35.968 50.858 1.000 20.621  ? 229 LEU   AAA C   1 ? 
ATOM   1790 O  O   . LEU   A 1 230 ? -0.745  34.789 50.432 1.000 26.366  ? 229 LEU   AAA O   1 ? 
ATOM   1791 C  CB  . LEU   A 1 230 ? -2.096  37.503 49.210 1.000 23.103  ? 229 LEU   AAA CB  1 ? 
ATOM   1792 C  CG  . LEU   A 1 230 ? -2.266  38.903 48.671 1.000 31.015  ? 229 LEU   AAA CG  1 ? 
ATOM   1793 C  CD1 . LEU   A 1 230 ? -3.519  38.960 47.807 1.000 31.823  ? 229 LEU   AAA CD1 1 ? 
ATOM   1794 C  CD2 . LEU   A 1 230 ? -2.322  39.923 49.810 1.000 28.660  ? 229 LEU   AAA CD2 1 ? 
ATOM   1795 N  N   . LEU   A 1 231 ? -1.417  36.237 52.084 1.000 20.569  ? 230 LEU   AAA N   1 ? 
ATOM   1796 C  CA  . LEU   A 1 231 ? -1.538  35.221 53.147 1.000 19.668  ? 230 LEU   AAA CA  1 ? 
ATOM   1797 C  C   . LEU   A 1 231 ? -3.007  34.900 53.399 1.000 19.457  ? 230 LEU   AAA C   1 ? 
ATOM   1798 O  O   . LEU   A 1 231 ? -3.859  35.825 53.533 1.000 21.788  ? 230 LEU   AAA O   1 ? 
ATOM   1799 C  CB  . LEU   A 1 231 ? -0.801  35.713 54.391 1.000 23.650  ? 230 LEU   AAA CB  1 ? 
ATOM   1800 C  CG  . LEU   A 1 231 ? 0.696   35.968 54.166 1.000 24.855  ? 230 LEU   AAA CG  1 ? 
ATOM   1801 C  CD1 . LEU   A 1 231 ? 1.324   36.547 55.414 1.000 28.531  ? 230 LEU   AAA CD1 1 ? 
ATOM   1802 C  CD2 . LEU   A 1 231 ? 1.453   34.698 53.716 1.000 26.022  ? 230 LEU   AAA CD2 1 ? 
ATOM   1803 N  N   . SER   A 1 232 ? -3.300  33.592 53.470 1.000 22.572  ? 231 SER   AAA N   1 ? 
ATOM   1804 C  CA  . SER   A 1 232 ? -4.678  33.087 53.729 1.000 21.594  ? 231 SER   AAA CA  1 ? 
ATOM   1805 C  C   . SER   A 1 232 ? -5.014  33.107 55.233 1.000 21.790  ? 231 SER   AAA C   1 ? 
ATOM   1806 O  O   . SER   A 1 232 ? -6.206  32.977 55.594 1.000 23.661  ? 231 SER   AAA O   1 ? 
ATOM   1807 C  CB  . SER   A 1 232 ? -4.870  31.705 53.176 1.000 26.149  ? 231 SER   AAA CB  1 ? 
ATOM   1808 O  OG  . SER   A 1 232 ? -3.858  30.823 53.669 1.000 28.159  ? 231 SER   AAA OG  1 ? 
ATOM   1809 N  N   . ASN   A 1 233 ? -3.988  33.154 56.075 1.000 21.220  ? 232 ASN   AAA N   1 ? 
ATOM   1810 C  CA  . ASN   A 1 233 ? -4.127  33.058 57.552 1.000 20.450  ? 232 ASN   AAA CA  1 ? 
ATOM   1811 C  C   . ASN   A 1 233 ? -4.449  34.456 58.083 1.000 18.704  ? 232 ASN   AAA C   1 ? 
ATOM   1812 O  O   . ASN   A 1 233 ? -4.101  35.473 57.364 1.000 24.599  ? 232 ASN   AAA O   1 ? 
ATOM   1813 C  CB  . ASN   A 1 233 ? -2.859  32.553 58.229 1.000 24.581  ? 232 ASN   AAA CB  1 ? 
ATOM   1814 C  CG  . ASN   A 1 233 ? -1.657  33.430 57.917 1.000 24.574  ? 232 ASN   AAA CG  1 ? 
ATOM   1815 O  OD1 . ASN   A 1 233 ? -1.203  34.219 58.749 1.000 27.958  ? 232 ASN   AAA OD1 1 ? 
ATOM   1816 N  ND2 . ASN   A 1 233 ? -1.144  33.312 56.715 1.000 18.882  ? 232 ASN   AAA ND2 1 ? 
ATOM   1817 N  N   . VAL   A 1 234 ? -5.000  34.508 59.302 1.000 22.534  ? 233 VAL   AAA N   1 ? 
ATOM   1818 C  CA  . VAL   A 1 234 ? -5.177  35.792 60.048 1.000 23.860  ? 233 VAL   AAA CA  1 ? 
ATOM   1819 C  C   . VAL   A 1 234 ? -3.834  36.163 60.673 1.000 19.085  ? 233 VAL   AAA C   1 ? 
ATOM   1820 O  O   . VAL   A 1 234 ? -2.957  35.270 60.891 1.000 24.933  ? 233 VAL   AAA O   1 ? 
ATOM   1821 C  CB  . VAL   A 1 234 ? -6.258  35.678 61.131 1.000 27.423  ? 233 VAL   AAA CB  1 ? 
ATOM   1822 C  CG1 . VAL   A 1 234 ? -7.603  35.282 60.539 1.000 30.278  ? 233 VAL   AAA CG1 1 ? 
ATOM   1823 C  CG2 . VAL   A 1 234 ? -5.832  34.712 62.227 1.000 32.394  ? 233 VAL   AAA CG2 1 ? 
ATOM   1824 N  N   . GLU   A 1 235 ? -3.671  37.434 60.938 1.000 21.093  ? 234 GLU   AAA N   1 ? 
ATOM   1825 C  CA  . GLU   A 1 235 ? -2.443  38.002 61.504 1.000 23.191  ? 234 GLU   AAA CA  1 ? 
ATOM   1826 C  C   . GLU   A 1 235 ? -2.108  37.260 62.791 1.000 24.836  ? 234 GLU   AAA C   1 ? 
ATOM   1827 O  O   . GLU   A 1 235 ? -3.040  37.018 63.597 1.000 23.766  ? 234 GLU   AAA O   1 ? 
ATOM   1828 C  CB  . GLU   A 1 235 ? -2.699  39.489 61.761 1.000 24.923  ? 234 GLU   AAA CB  1 ? 
ATOM   1829 C  CG  . GLU   A 1 235 ? -1.518  40.227 62.379 1.000 25.785  ? 234 GLU   AAA CG  1 ? 
ATOM   1830 C  CD  . GLU   A 1 235 ? -1.693  41.734 62.425 1.000 30.511  ? 234 GLU   AAA CD  1 ? 
ATOM   1831 O  OE1 . GLU   A 1 235 ? -1.860  42.356 61.374 1.000 30.312  ? 234 GLU   AAA OE1 1 ? 
ATOM   1832 O  OE2 . GLU   A 1 235 ? -1.635  42.255 63.511 1.000 39.919  ? 234 GLU   AAA OE2 1 ? 
ATOM   1833 N  N   . GLY   A 1 236 ? -0.828  36.937 62.970 1.000 25.323  ? 235 GLY   AAA N   1 ? 
ATOM   1834 C  CA  . GLY   A 1 236 ? -0.318  36.297 64.194 1.000 24.441  ? 235 GLY   AAA CA  1 ? 
ATOM   1835 C  C   . GLY   A 1 236 ? -0.288  34.790 64.026 1.000 29.446  ? 235 GLY   AAA C   1 ? 
ATOM   1836 O  O   . GLY   A 1 236 ? 0.438   34.155 64.778 1.000 37.284  ? 235 GLY   AAA O   1 ? 
ATOM   1837 N  N   . ASP   A 1 237 ? -1.049  34.214 63.088 1.000 26.346  ? 236 ASP   AAA N   1 ? 
ATOM   1838 C  CA  . ASP   A 1 237 ? -0.965  32.745 62.842 1.000 28.624  ? 236 ASP   AAA CA  1 ? 
ATOM   1839 C  C   . ASP   A 1 237 ? 0.251   32.481 61.949 1.000 30.905  ? 236 ASP   AAA C   1 ? 
ATOM   1840 O  O   . ASP   A 1 237 ? 0.832   33.459 61.410 1.000 33.763  ? 236 ASP   AAA O   1 ? 
ATOM   1841 C  CB  . ASP   A 1 237 ? -2.256  32.186 62.238 1.000 29.395  ? 236 ASP   AAA CB  1 ? 
ATOM   1842 C  CG  . ASP   A 1 237 ? -3.377  32.030 63.244 1.000 31.948  ? 236 ASP   AAA CG  1 ? 
ATOM   1843 O  OD1 . ASP   A 1 237 ? -3.125  32.274 64.446 1.000 37.774  ? 236 ASP   AAA OD1 1 ? 
ATOM   1844 O  OD2 . ASP   A 1 237 ? -4.489  31.634 62.821 1.000 36.857  ? 236 ASP   AAA OD2 1 ? 
ATOM   1845 N  N   . ASN   A 1 238 ? 0.670   31.218 61.821 1.000 30.037  ? 237 ASN   AAA N   1 ? 
ATOM   1846 C  CA  A ASN   A 1 238 ? 1.803   30.942 60.890 0.500 31.493  ? 237 ASN   AAA CA  1 ? 
ATOM   1847 C  CA  B ASN   A 1 238 ? 1.713   30.765 60.863 0.500 34.651  ? 237 ASN   AAA CA  1 ? 
ATOM   1848 C  C   . ASN   A 1 238 ? 1.321   31.242 59.463 1.000 30.520  ? 237 ASN   AAA C   1 ? 
ATOM   1849 O  O   . ASN   A 1 238 ? 0.125   31.045 59.106 1.000 29.015  ? 237 ASN   AAA O   1 ? 
ATOM   1850 C  CB  A ASN   A 1 238 ? 2.494   29.574 61.034 0.500 34.400  ? 237 ASN   AAA CB  1 ? 
ATOM   1851 C  CB  B ASN   A 1 238 ? 1.861   29.243 60.919 0.500 34.476  ? 237 ASN   AAA CB  1 ? 
ATOM   1852 C  CG  A ASN   A 1 238 ? 3.882   29.515 60.394 0.500 33.583  ? 237 ASN   AAA CG  1 ? 
ATOM   1853 C  CG  B ASN   A 1 238 ? 2.337   28.785 62.283 0.500 35.977  ? 237 ASN   AAA CG  1 ? 
ATOM   1854 O  OD1 A ASN   A 1 238 ? 4.897   29.280 61.068 0.500 32.386  ? 237 ASN   AAA OD1 1 ? 
ATOM   1855 O  OD1 B ASN   A 1 238 ? 2.996   29.555 62.983 0.500 42.347  ? 237 ASN   AAA OD1 1 ? 
ATOM   1856 N  ND2 A ASN   A 1 238 ? 3.956   29.680 59.072 0.500 38.220  ? 237 ASN   AAA ND2 1 ? 
ATOM   1857 N  ND2 B ASN   A 1 238 ? 1.983   27.573 62.680 0.500 34.300  ? 237 ASN   AAA ND2 1 ? 
ATOM   1858 N  N   . ALA   A 1 239 ? 2.250   31.790 58.696 1.000 34.873  ? 238 ALA   AAA N   1 ? 
ATOM   1859 C  CA  . ALA   A 1 239 ? 1.990   32.287 57.329 1.000 32.910  ? 238 ALA   AAA CA  1 ? 
ATOM   1860 C  C   . ALA   A 1 239 ? 1.604   31.116 56.405 1.000 30.263  ? 238 ALA   AAA C   1 ? 
ATOM   1861 O  O   . ALA   A 1 239 ? 2.271   30.072 56.440 1.000 36.145  ? 238 ALA   AAA O   1 ? 
ATOM   1862 C  CB  . ALA   A 1 239 ? 3.205   33.039 56.857 1.000 38.003  ? 238 ALA   AAA CB  1 ? 
ATOM   1863 N  N   . VAL   A 1 240 ? 0.510   31.254 55.658 1.000 26.754  ? 239 VAL   AAA N   1 ? 
ATOM   1864 C  CA  . VAL   A 1 240 ? 0.055   30.260 54.649 1.000 27.546  ? 239 VAL   AAA CA  1 ? 
ATOM   1865 C  C   . VAL   A 1 240 ? -0.201  31.036 53.360 1.000 26.673  ? 239 VAL   AAA C   1 ? 
ATOM   1866 O  O   . VAL   A 1 240 ? -1.282  31.621 53.197 1.000 27.794  ? 239 VAL   AAA O   1 ? 
ATOM   1867 C  CB  . VAL   A 1 240 ? -1.194  29.490 55.127 1.000 29.268  ? 239 VAL   AAA CB  1 ? 
ATOM   1868 C  CG1 . VAL   A 1 240 ? -1.640  28.476 54.090 1.000 31.576  ? 239 VAL   AAA CG1 1 ? 
ATOM   1869 C  CG2 . VAL   A 1 240 ? -1.012  28.866 56.500 1.000 30.653  ? 239 VAL   AAA CG2 1 ? 
ATOM   1870 N  N   . PRO   A 1 241 ? 0.828   31.139 52.483 1.000 26.966  ? 240 PRO   AAA N   1 ? 
ATOM   1871 C  CA  . PRO   A 1 241 ? 0.696   31.796 51.183 1.000 22.983  ? 240 PRO   AAA CA  1 ? 
ATOM   1872 C  C   . PRO   A 1 241 ? -0.503  31.303 50.356 1.000 26.598  ? 240 PRO   AAA C   1 ? 
ATOM   1873 O  O   . PRO   A 1 241 ? -0.797  30.138 50.426 1.000 29.102  ? 240 PRO   AAA O   1 ? 
ATOM   1874 C  CB  . PRO   A 1 241 ? 2.032   31.526 50.490 1.000 31.721  ? 240 PRO   AAA CB  1 ? 
ATOM   1875 C  CG  . PRO   A 1 241 ? 2.997   31.353 51.638 1.000 35.500  ? 240 PRO   AAA CG  1 ? 
ATOM   1876 C  CD  . PRO   A 1 241 ? 2.192   30.611 52.685 1.000 31.711  ? 240 PRO   AAA CD  1 ? 
ATOM   1877 N  N   . MET   A 1 242 ? -1.204  32.256 49.716 1.000 24.129  ? 241 MET   AAA N   1 ? 
ATOM   1878 C  CA  . MET   A 1 242 ? -2.306  32.064 48.740 1.000 25.115  ? 241 MET   AAA CA  1 ? 
ATOM   1879 C  C   . MET   A 1 242 ? -1.721  31.505 47.436 1.000 24.359  ? 241 MET   AAA C   1 ? 
ATOM   1880 O  O   . MET   A 1 242 ? -1.623  32.227 46.476 1.000 28.721  ? 241 MET   AAA O   1 ? 
ATOM   1881 C  CB  . MET   A 1 242 ? -3.013  33.377 48.424 1.000 30.474  ? 241 MET   AAA CB  1 ? 
ATOM   1882 C  CG  . MET   A 1 242 ? -4.148  33.627 49.302 1.000 35.067  ? 241 MET   AAA CG  1 ? 
ATOM   1883 S  SD  . MET   A 1 242 ? -5.011  35.067 48.709 1.000 28.530  ? 241 MET   AAA SD  1 ? 
ATOM   1884 C  CE  . MET   A 1 242 ? -5.437  35.731 50.318 1.000 24.761  ? 241 MET   AAA CE  1 ? 
ATOM   1885 N  N   . GLN   A 1 243 ? -1.338  30.237 47.381 1.000 23.168  ? 242 GLN   AAA N   1 ? 
ATOM   1886 C  CA  . GLN   A 1 243 ? -0.577  29.766 46.182 1.000 25.582  ? 242 GLN   AAA CA  1 ? 
ATOM   1887 C  C   . GLN   A 1 243 ? -1.460  29.653 44.923 1.000 22.535  ? 242 GLN   AAA C   1 ? 
ATOM   1888 O  O   . GLN   A 1 243 ? -0.888  29.807 43.835 1.000 24.323  ? 242 GLN   AAA O   1 ? 
ATOM   1889 C  CB  . GLN   A 1 243 ? 0.086   28.425 46.469 1.000 33.605  ? 242 GLN   AAA CB  1 ? 
ATOM   1890 C  CG  . GLN   A 1 243 ? 1.183   28.523 47.528 1.000 41.472  ? 242 GLN   AAA CG  1 ? 
ATOM   1891 C  CD  . GLN   A 1 243 ? 2.034   27.276 47.557 1.000 38.287  ? 242 GLN   AAA CD  1 ? 
ATOM   1892 O  OE1 . GLN   A 1 243 ? 2.537   26.826 46.535 1.000 45.055  ? 242 GLN   AAA OE1 1 ? 
ATOM   1893 N  NE2 . GLN   A 1 243 ? 2.198   26.707 48.740 1.000 53.733  ? 242 GLN   AAA NE2 1 ? 
ATOM   1894 N  N   . HIS   A 1 244 ? -2.757  29.294 45.041 1.000 26.362  ? 243 HIS   AAA N   1 ? 
ATOM   1895 C  CA  . HIS   A 1 244 ? -3.652  29.089 43.866 1.000 23.463  ? 243 HIS   AAA CA  1 ? 
ATOM   1896 C  C   . HIS   A 1 244 ? -5.133  29.225 44.258 1.000 22.213  ? 243 HIS   AAA C   1 ? 
ATOM   1897 O  O   . HIS   A 1 244 ? -5.467  29.031 45.434 1.000 20.839  ? 243 HIS   AAA O   1 ? 
ATOM   1898 C  CB  . HIS   A 1 244 ? -3.361  27.726 43.199 1.000 28.209  ? 243 HIS   AAA CB  1 ? 
ATOM   1899 C  CG  . HIS   A 1 244 ? -3.618  26.574 44.110 1.000 33.252  ? 243 HIS   AAA CG  1 ? 
ATOM   1900 N  ND1 . HIS   A 1 244 ? -4.804  25.845 44.093 1.000 37.565  ? 243 HIS   AAA ND1 1 ? 
ATOM   1901 C  CD2 . HIS   A 1 244 ? -2.860  26.038 45.097 1.000 35.598  ? 243 HIS   AAA CD2 1 ? 
ATOM   1902 C  CE1 . HIS   A 1 244 ? -4.762  24.915 45.029 1.000 38.157  ? 243 HIS   AAA CE1 1 ? 
ATOM   1903 N  NE2 . HIS   A 1 244 ? -3.583  25.017 45.663 1.000 36.895  ? 243 HIS   AAA NE2 1 ? 
ATOM   1904 N  N   . ASN   A 1 245 ? -5.992  29.551 43.289 1.000 20.424  ? 244 ASN   AAA N   1 ? 
ATOM   1905 C  CA  . ASN   A 1 245 ? -7.456  29.723 43.532 1.000 19.750  ? 244 ASN   AAA CA  1 ? 
ATOM   1906 C  C   . ASN   A 1 245 ? -8.256  29.580 42.220 1.000 20.206  ? 244 ASN   AAA C   1 ? 
ATOM   1907 O  O   . ASN   A 1 245 ? -9.361  30.230 42.062 1.000 23.109  ? 244 ASN   AAA O   1 ? 
ATOM   1908 C  CB  . ASN   A 1 245 ? -7.711  31.042 44.260 1.000 20.831  ? 244 ASN   AAA CB  1 ? 
ATOM   1909 C  CG  . ASN   A 1 245 ? -7.158  32.217 43.495 1.000 19.406  ? 244 ASN   AAA CG  1 ? 
ATOM   1910 O  OD1 . ASN   A 1 245 ? -6.797  32.069 42.321 1.000 19.168  ? 244 ASN   AAA OD1 1 ? 
ATOM   1911 N  ND2 . ASN   A 1 245 ? -7.131  33.398 44.176 1.000 20.744  ? 244 ASN   AAA ND2 1 ? 
ATOM   1912 N  N   . ASN   A 1 246 ? -7.737  28.743 41.302 1.000 18.900  ? 245 ASN   AAA N   1 ? 
ATOM   1913 C  CA  . ASN   A 1 246 ? -8.368  28.481 39.994 1.000 21.140  ? 245 ASN   AAA CA  1 ? 
ATOM   1914 C  C   . ASN   A 1 246 ? -9.096  27.130 40.053 1.000 19.642  ? 245 ASN   AAA C   1 ? 
ATOM   1915 O  O   . ASN   A 1 246 ? -8.521  26.130 40.446 1.000 25.588  ? 245 ASN   AAA O   1 ? 
ATOM   1916 C  CB  . ASN   A 1 246 ? -7.439  28.620 38.790 1.000 22.234  ? 245 ASN   AAA CB  1 ? 
ATOM   1917 C  CG  . ASN   A 1 246 ? -6.326  27.574 38.734 1.000 23.075  ? 245 ASN   AAA CG  1 ? 
ATOM   1918 O  OD1 . ASN   A 1 246 ? -5.945  27.095 37.653 1.000 30.136  ? 245 ASN   AAA OD1 1 ? 
ATOM   1919 N  ND2 . ASN   A 1 246 ? -5.696  27.350 39.869 1.000 20.441  ? 245 ASN   AAA ND2 1 ? 
ATOM   1920 N  N   . ARG   A 1 247 ? -10.338 27.172 39.632 1.000 19.105  ? 246 ARG   AAA N   1 ? 
ATOM   1921 C  CA  . ARG   A 1 247 ? -11.169 25.985 39.520 1.000 20.804  ? 246 ARG   AAA CA  1 ? 
ATOM   1922 C  C   . ARG   A 1 247 ? -10.855 25.355 38.179 1.000 22.248  ? 246 ARG   AAA C   1 ? 
ATOM   1923 O  O   . ARG   A 1 247 ? -10.754 26.001 37.128 1.000 23.690  ? 246 ARG   AAA O   1 ? 
ATOM   1924 C  CB  . ARG   A 1 247 ? -12.658 26.330 39.530 1.000 20.071  ? 246 ARG   AAA CB  1 ? 
ATOM   1925 C  CG  . ARG   A 1 247 ? -13.562 25.125 39.678 1.000 21.751  ? 246 ARG   AAA CG  1 ? 
ATOM   1926 C  CD  . ARG   A 1 247 ? -15.005 25.347 39.333 1.000 22.219  ? 246 ARG   AAA CD  1 ? 
ATOM   1927 N  NE  . ARG   A 1 247 ? -15.876 24.270 39.815 1.000 21.730  ? 246 ARG   AAA NE  1 ? 
ATOM   1928 C  CZ  . ARG   A 1 247 ? -17.178 24.211 39.609 1.000 22.647  ? 246 ARG   AAA CZ  1 ? 
ATOM   1929 N  NH1 . ARG   A 1 247 ? -17.789 25.119 38.861 1.000 23.834  ? 246 ARG   AAA NH1 1 ? 
ATOM   1930 N  NH2 . ARG   A 1 247 ? -17.880 23.206 40.101 1.000 25.967  ? 246 ARG   AAA NH2 1 ? 
ATOM   1931 N  N   . PRO   A 1 248 ? -10.781 23.992 38.127 1.000 23.069  ? 247 PRO   AAA N   1 ? 
ATOM   1932 C  CA  . PRO   A 1 248 ? -10.677 23.351 36.827 1.000 26.061  ? 247 PRO   AAA CA  1 ? 
ATOM   1933 C  C   . PRO   A 1 248 ? -11.889 23.650 35.932 1.000 24.595  ? 247 PRO   AAA C   1 ? 
ATOM   1934 O  O   . PRO   A 1 248 ? -12.983 23.929 36.505 1.000 28.703  ? 247 PRO   AAA O   1 ? 
ATOM   1935 C  CB  . PRO   A 1 248 ? -10.752 21.850 37.142 1.000 24.595  ? 247 PRO   AAA CB  1 ? 
ATOM   1936 C  CG  . PRO   A 1 248 ? -10.343 21.756 38.596 1.000 31.475  ? 247 PRO   AAA CG  1 ? 
ATOM   1937 C  CD  . PRO   A 1 248 ? -10.807 23.046 39.259 1.000 26.264  ? 247 PRO   AAA CD  1 ? 
ATOM   1938 N  N   . THR   A 1 249 ? -11.707 23.465 34.622 1.000 23.366  ? 248 THR   AAA N   1 ? 
ATOM   1939 C  CA  . THR   A 1 249 ? -12.800 23.544 33.600 1.000 23.920  ? 248 THR   AAA CA  1 ? 
ATOM   1940 C  C   . THR   A 1 249 ? -13.801 22.376 33.793 1.000 23.760  ? 248 THR   AAA C   1 ? 
ATOM   1941 O  O   . THR   A 1 249 ? -13.431 21.223 34.210 1.000 24.919  ? 248 THR   AAA O   1 ? 
ATOM   1942 C  CB  . THR   A 1 249 ? -12.227 23.664 32.177 1.000 25.725  ? 248 THR   AAA CB  1 ? 
ATOM   1943 O  OG1 . THR   A 1 249 ? -11.439 22.489 31.879 1.000 24.021  ? 248 THR   AAA OG1 1 ? 
ATOM   1944 C  CG2 . THR   A 1 249 ? -11.455 24.978 32.027 1.000 24.163  ? 248 THR   AAA CG2 1 ? 
ATOM   1945 N  N   . GLN   A 1 250 ? -15.048 22.702 33.493 1.000 22.796  ? 249 GLN   AAA N   1 ? 
ATOM   1946 C  CA  . GLN   A 1 250 ? -16.250 21.917 33.797 1.000 22.592  ? 249 GLN   AAA CA  1 ? 
ATOM   1947 C  C   . GLN   A 1 250 ? -16.906 21.589 32.465 1.000 25.216  ? 249 GLN   AAA C   1 ? 
ATOM   1948 O  O   . GLN   A 1 250 ? -16.705 22.228 31.433 1.000 26.559  ? 249 GLN   AAA O   1 ? 
ATOM   1949 C  CB  . GLN   A 1 250 ? -17.189 22.705 34.717 1.000 23.518  ? 249 GLN   AAA CB  1 ? 
ATOM   1950 C  CG  . GLN   A 1 250 ? -16.534 23.149 36.023 1.000 24.519  ? 249 GLN   AAA CG  1 ? 
ATOM   1951 C  CD  . GLN   A 1 250 ? -15.999 21.999 36.855 1.000 24.834  ? 249 GLN   AAA CD  1 ? 
ATOM   1952 O  OE1 . GLN   A 1 250 ? -14.881 22.004 37.380 1.000 28.275  ? 249 GLN   AAA OE1 1 ? 
ATOM   1953 N  NE2 . GLN   A 1 250 ? -16.795 20.963 36.959 1.000 25.749  ? 249 GLN   AAA NE2 1 ? 
ATOM   1954 N  N   . PRO   A 1 251 ? -17.669 20.488 32.432 1.000 33.233  ? 250 PRO   AAA N   1 ? 
ATOM   1955 C  CA  . PRO   A 1 251 ? -18.267 20.051 31.181 1.000 31.562  ? 250 PRO   AAA CA  1 ? 
ATOM   1956 C  C   . PRO   A 1 251 ? -19.311 21.022 30.606 1.000 26.741  ? 250 PRO   AAA C   1 ? 
ATOM   1957 O  O   . PRO   A 1 251 ? -20.127 21.503 31.360 1.000 28.731  ? 250 PRO   AAA O   1 ? 
ATOM   1958 C  CB  . PRO   A 1 251 ? -18.977 18.743 31.541 1.000 34.471  ? 250 PRO   AAA CB  1 ? 
ATOM   1959 C  CG  . PRO   A 1 251 ? -18.561 18.401 32.955 1.000 33.391  ? 250 PRO   AAA CG  1 ? 
ATOM   1960 C  CD  . PRO   A 1 251 ? -17.930 19.615 33.583 1.000 31.214  ? 250 PRO   AAA CD  1 ? 
ATOM   1961 N  N   . LEU   A 1 252 ? -19.242 21.286 29.306 1.000 27.122  ? 251 LEU   AAA N   1 ? 
ATOM   1962 C  CA  . LEU   A 1 252 ? -20.271 22.164 28.638 1.000 31.438  ? 251 LEU   AAA CA  1 ? 
ATOM   1963 C  C   . LEU   A 1 252 ? -21.670 21.545 28.762 1.000 34.143  ? 251 LEU   AAA C   1 ? 
ATOM   1964 O  O   . LEU   A 1 252 ? -22.625 22.386 28.837 1.000 34.299  ? 251 LEU   AAA O   1 ? 
ATOM   1965 C  CB  . LEU   A 1 252 ? -19.885 22.400 27.177 1.000 37.495  ? 251 LEU   AAA CB  1 ? 
ATOM   1966 C  CG  . LEU   A 1 252 ? -18.902 23.540 26.954 1.000 41.401  ? 251 LEU   AAA CG  1 ? 
ATOM   1967 C  CD1 . LEU   A 1 252 ? -18.377 23.495 25.537 1.000 48.994  ? 251 LEU   AAA CD1 1 ? 
ATOM   1968 C  CD2 . LEU   A 1 252 ? -19.569 24.872 27.230 1.000 35.587  ? 251 LEU   AAA CD2 1 ? 
ATOM   1969 N  N   . LYS   A 1 253 ? -21.822 20.214 28.782 1.000 35.735  ? 252 LYS   AAA N   1 ? 
ATOM   1970 C  CA  . LYS   A 1 253 ? -23.197 19.669 28.878 1.000 35.081  ? 252 LYS   AAA CA  1 ? 
ATOM   1971 C  C   . LYS   A 1 253 ? -24.140 20.345 27.888 1.000 29.608  ? 252 LYS   AAA C   1 ? 
ATOM   1972 O  O   . LYS   A 1 253 ? -25.262 20.585 28.278 1.000 38.619  ? 252 LYS   AAA O   1 ? 
ATOM   1973 C  CB  . LYS   A 1 253 ? -23.763 19.836 30.296 1.000 33.982  ? 252 LYS   AAA CB  1 ? 
ATOM   1974 C  CG  . LYS   A 1 253 ? -22.971 19.187 31.423 1.000 37.339  ? 252 LYS   AAA CG  1 ? 
ATOM   1975 C  CD  . LYS   A 1 253 ? -23.441 17.803 31.779 1.000 44.285  ? 252 LYS   AAA CD  1 ? 
ATOM   1976 C  CE  . LYS   A 1 253 ? -22.680 17.220 32.948 1.000 55.969  ? 252 LYS   AAA CE  1 ? 
ATOM   1977 N  NZ  . LYS   A 1 253 ? -23.303 15.955 33.403 1.000 69.228  ? 252 LYS   AAA NZ  1 ? 
ATOM   1978 N  N   . GLY   A 1 254 ? -23.681 20.496 26.612 1.000 33.847  ? 253 GLY   AAA N   1 ? 
ATOM   1979 C  CA  . GLY   A 1 254 ? -24.528 20.866 25.460 1.000 37.145  ? 253 GLY   AAA CA  1 ? 
ATOM   1980 C  C   . GLY   A 1 254 ? -24.676 22.361 25.300 1.000 35.123  ? 253 GLY   AAA C   1 ? 
ATOM   1981 O  O   . GLY   A 1 254 ? -25.395 22.757 24.361 1.000 34.849  ? 253 GLY   AAA O   1 ? 
ATOM   1982 N  N   . ARG   A 1 255 ? -24.029 23.173 26.150 1.000 31.532  ? 254 ARG   AAA N   1 ? 
ATOM   1983 C  CA  . ARG   A 1 255 ? -24.090 24.639 25.985 1.000 29.710  ? 254 ARG   AAA CA  1 ? 
ATOM   1984 C  C   . ARG   A 1 255 ? -23.312 25.015 24.734 1.000 32.017  ? 254 ARG   AAA C   1 ? 
ATOM   1985 O  O   . ARG   A 1 255 ? -22.355 24.290 24.368 1.000 34.284  ? 254 ARG   AAA O   1 ? 
ATOM   1986 C  CB  . ARG   A 1 255 ? -23.493 25.402 27.172 1.000 29.558  ? 254 ARG   AAA CB  1 ? 
ATOM   1987 C  CG  . ARG   A 1 255 ? -24.330 25.289 28.429 1.000 30.059  ? 254 ARG   AAA CG  1 ? 
ATOM   1988 C  CD  . ARG   A 1 255 ? -23.619 25.895 29.598 1.000 27.390  ? 254 ARG   AAA CD  1 ? 
ATOM   1989 N  NE  . ARG   A 1 255 ? -22.610 25.013 30.136 1.000 27.162  ? 254 ARG   AAA NE  1 ? 
ATOM   1990 C  CZ  . ARG   A 1 255 ? -21.781 25.332 31.106 1.000 23.952  ? 254 ARG   AAA CZ  1 ? 
ATOM   1991 N  NH1 . ARG   A 1 255 ? -21.744 26.576 31.571 1.000 27.796  ? 254 ARG   AAA NH1 1 ? 
ATOM   1992 N  NH2 . ARG   A 1 255 ? -20.900 24.452 31.532 1.000 23.862  ? 254 ARG   AAA NH2 1 ? 
ATOM   1993 N  N   . THR   A 1 256 ? -23.679 26.161 24.160 1.000 29.556  ? 255 THR   AAA N   1 ? 
ATOM   1994 C  CA  . THR   A 1 256 ? -23.030 26.729 22.959 1.000 30.192  ? 255 THR   AAA CA  1 ? 
ATOM   1995 C  C   . THR   A 1 256 ? -22.236 27.955 23.411 1.000 26.387  ? 255 THR   AAA C   1 ? 
ATOM   1996 O  O   . THR   A 1 256 ? -22.829 28.828 24.095 1.000 33.044  ? 255 THR   AAA O   1 ? 
ATOM   1997 C  CB  . THR   A 1 256 ? -24.087 27.087 21.912 1.000 38.245  ? 255 THR   AAA CB  1 ? 
ATOM   1998 O  OG1 . THR   A 1 256 ? -24.688 25.851 21.551 1.000 42.127  ? 255 THR   AAA OG1 1 ? 
ATOM   1999 C  CG2 . THR   A 1 256 ? -23.526 27.762 20.682 1.000 42.923  ? 255 THR   AAA CG2 1 ? 
ATOM   2000 N  N   . VAL   A 1 257 ? -20.944 27.989 23.092 1.000 27.948  ? 256 VAL   AAA N   1 ? 
ATOM   2001 C  CA  . VAL   A 1 257 ? -20.127 29.224 23.244 1.000 27.296  ? 256 VAL   AAA CA  1 ? 
ATOM   2002 C  C   . VAL   A 1 257 ? -20.278 30.049 21.961 1.000 30.174  ? 256 VAL   AAA C   1 ? 
ATOM   2003 O  O   . VAL   A 1 257 ? -19.968 29.572 20.880 1.000 26.727  ? 256 VAL   AAA O   1 ? 
ATOM   2004 C  CB  . VAL   A 1 257 ? -18.657 28.909 23.577 1.000 29.384  ? 256 VAL   AAA CB  1 ? 
ATOM   2005 C  CG1 . VAL   A 1 257 ? -17.869 30.190 23.814 1.000 24.881  ? 256 VAL   AAA CG1 1 ? 
ATOM   2006 C  CG2 . VAL   A 1 257 ? -18.529 27.955 24.770 1.000 31.501  ? 256 VAL   AAA CG2 1 ? 
ATOM   2007 N  N   . ARG   A 1 258 ? -20.769 31.279 22.082 1.000 27.997  ? 257 ARG   AAA N   1 ? 
ATOM   2008 C  CA  . ARG   A 1 258 ? -20.944 32.181 20.915 1.000 27.396  ? 257 ARG   AAA CA  1 ? 
ATOM   2009 C  C   . ARG   A 1 258 ? -19.718 33.069 20.808 1.000 22.448  ? 257 ARG   AAA C   1 ? 
ATOM   2010 O  O   . ARG   A 1 258 ? -19.135 33.417 21.872 1.000 29.830  ? 257 ARG   AAA O   1 ? 
ATOM   2011 C  CB  . ARG   A 1 258 ? -22.228 32.996 21.049 1.000 27.230  ? 257 ARG   AAA CB  1 ? 
ATOM   2012 C  CG  . ARG   A 1 258 ? -23.464 32.119 20.969 1.000 32.605  ? 257 ARG   AAA CG  1 ? 
ATOM   2013 C  CD  . ARG   A 1 258 ? -24.745 32.907 21.096 1.000 33.865  ? 257 ARG   AAA CD  1 ? 
ATOM   2014 N  NE  . ARG   A 1 258 ? -24.898 33.439 22.444 1.000 34.302  ? 257 ARG   AAA NE  1 ? 
ATOM   2015 C  CZ  . ARG   A 1 258 ? -25.643 34.488 22.773 1.000 31.703  ? 257 ARG   AAA CZ  1 ? 
ATOM   2016 N  NH1 . ARG   A 1 258 ? -26.298 35.163 21.851 1.000 37.890  ? 257 ARG   AAA NH1 1 ? 
ATOM   2017 N  NH2 . ARG   A 1 258 ? -25.731 34.867 24.031 1.000 35.262  ? 257 ARG   AAA NH2 1 ? 
ATOM   2018 N  N   . ALA   A 1 259 ? -19.371 33.441 19.578 1.000 26.585  ? 258 ALA   AAA N   1 ? 
ATOM   2019 C  CA  . ALA   A 1 259 ? -18.258 34.369 19.266 1.000 28.876  ? 258 ALA   AAA CA  1 ? 
ATOM   2020 C  C   . ALA   A 1 259 ? -18.837 35.669 18.691 1.000 27.807  ? 258 ALA   AAA C   1 ? 
ATOM   2021 O  O   . ALA   A 1 259 ? -19.769 35.630 17.894 1.000 30.302  ? 258 ALA   AAA O   1 ? 
ATOM   2022 C  CB  . ALA   A 1 259 ? -17.289 33.684 18.319 1.000 28.849  ? 258 ALA   AAA CB  1 ? 
ATOM   2023 N  N   . SER   A 1 260 ? -18.316 36.802 19.132 1.000 25.829  ? 259 SER   AAA N   1 ? 
ATOM   2024 C  CA  . SER   A 1 260 ? -18.678 38.145 18.604 1.000 28.037  ? 259 SER   AAA CA  1 ? 
ATOM   2025 C  C   . SER   A 1 260 ? -17.916 38.422 17.305 1.000 31.729  ? 259 SER   AAA C   1 ? 
ATOM   2026 O  O   . SER   A 1 260 ? -18.180 39.491 16.649 1.000 33.424  ? 259 SER   AAA O   1 ? 
ATOM   2027 C  CB  . SER   A 1 260 ? -18.347 39.173 19.633 1.000 28.529  ? 259 SER   AAA CB  1 ? 
ATOM   2028 O  OG  . SER   A 1 260 ? -16.952 39.412 19.669 1.000 29.910  ? 259 SER   AAA OG  1 ? 
ATOM   2029 N  N   . PHE   A 1 261 ? -16.972 37.537 16.967 1.000 32.173  ? 260 PHE   AAA N   1 ? 
ATOM   2030 C  CA  . PHE   A 1 261 ? -15.959 37.754 15.903 1.000 32.313  ? 260 PHE   AAA CA  1 ? 
ATOM   2031 C  C   . PHE   A 1 261 ? -15.793 36.466 15.080 1.000 37.553  ? 260 PHE   AAA C   1 ? 
ATOM   2032 O  O   . PHE   A 1 261 ? -15.255 36.546 13.977 1.000 41.025  ? 260 PHE   AAA O   1 ? 
ATOM   2033 C  CB  . PHE   A 1 261 ? -14.647 38.188 16.554 1.000 33.879  ? 260 PHE   AAA CB  1 ? 
ATOM   2034 C  CG  . PHE   A 1 261 ? -13.998 37.097 17.378 1.000 30.160  ? 260 PHE   AAA CG  1 ? 
ATOM   2035 C  CD1 . PHE   A 1 261 ? -14.382 36.885 18.688 1.000 28.224  ? 260 PHE   AAA CD1 1 ? 
ATOM   2036 C  CD2 . PHE   A 1 261 ? -13.024 36.275 16.833 1.000 36.338  ? 260 PHE   AAA CD2 1 ? 
ATOM   2037 C  CE1 . PHE   A 1 261 ? -13.811 35.880 19.443 1.000 31.036  ? 260 PHE   AAA CE1 1 ? 
ATOM   2038 C  CE2 . PHE   A 1 261 ? -12.454 35.260 17.591 1.000 38.685  ? 260 PHE   AAA CE2 1 ? 
ATOM   2039 C  CZ  . PHE   A 1 261 ? -12.843 35.070 18.898 1.000 32.083  ? 260 PHE   AAA CZ  1 ? 
ATOM   2040 O  OXT . PHE   A 1 261 ? -16.176 35.353 15.496 1.000 36.635  ? 260 PHE   AAA OXT 1 ? 
ATOM   2041 N  N   . SER   B 1 3   ? 28.319  30.986 38.976 1.000 57.734  ? 2   SER   BBB N   1 ? 
ATOM   2042 C  CA  . SER   B 1 3   ? 28.863  30.780 40.386 1.000 51.138  ? 2   SER   BBB CA  1 ? 
ATOM   2043 C  C   . SER   B 1 3   ? 28.567  29.363 40.901 1.000 45.411  ? 2   SER   BBB C   1 ? 
ATOM   2044 O  O   . SER   B 1 3   ? 27.600  28.731 40.467 1.000 40.694  ? 2   SER   BBB O   1 ? 
ATOM   2045 C  CB  . SER   B 1 3   ? 28.336  31.839 41.336 1.000 47.252  ? 2   SER   BBB CB  1 ? 
ATOM   2046 O  OG  . SER   B 1 3   ? 26.953  32.116 41.106 1.000 63.475  ? 2   SER   BBB OG  1 ? 
ATOM   2047 N  N   . PRO   B 1 4   ? 29.398  28.803 41.825 1.000 46.675  ? 3   PRO   BBB N   1 ? 
ATOM   2048 C  CA  . PRO   B 1 4   ? 29.233  27.422 42.304 1.000 46.787  ? 3   PRO   BBB CA  1 ? 
ATOM   2049 C  C   . PRO   B 1 4   ? 27.823  27.051 42.806 1.000 42.635  ? 3   PRO   BBB C   1 ? 
ATOM   2050 O  O   . PRO   B 1 4   ? 27.145  27.893 43.416 1.000 51.100  ? 3   PRO   BBB O   1 ? 
ATOM   2051 C  CB  . PRO   B 1 4   ? 30.261  27.325 43.446 1.000 51.697  ? 3   PRO   BBB CB  1 ? 
ATOM   2052 C  CG  . PRO   B 1 4   ? 31.349  28.285 43.023 1.000 51.548  ? 3   PRO   BBB CG  1 ? 
ATOM   2053 C  CD  . PRO   B 1 4   ? 30.589  29.446 42.412 1.000 48.330  ? 3   PRO   BBB CD  1 ? 
ATOM   2054 N  N   . ASP   B 1 5   ? 27.410  25.805 42.545 1.000 43.967  ? 4   ASP   BBB N   1 ? 
ATOM   2055 C  CA  . ASP   B 1 5   ? 26.036  25.304 42.822 1.000 38.506  ? 4   ASP   BBB CA  1 ? 
ATOM   2056 C  C   . ASP   B 1 5   ? 25.967  24.772 44.262 1.000 34.046  ? 4   ASP   BBB C   1 ? 
ATOM   2057 O  O   . ASP   B 1 5   ? 26.157  23.508 44.505 1.000 38.940  ? 4   ASP   BBB O   1 ? 
ATOM   2058 C  CB  . ASP   B 1 5   ? 25.617  24.265 41.776 1.000 41.414  ? 4   ASP   BBB CB  1 ? 
ATOM   2059 C  CG  . ASP   B 1 5   ? 24.185  23.747 41.929 1.000 55.977  ? 4   ASP   BBB CG  1 ? 
ATOM   2060 O  OD1 . ASP   B 1 5   ? 23.335  24.433 42.596 1.000 45.728  ? 4   ASP   BBB OD1 1 ? 
ATOM   2061 O  OD2 . ASP   B 1 5   ? 23.919  22.649 41.374 1.000 66.917  ? 4   ASP   BBB OD2 1 ? 
ATOM   2062 N  N   . TRP   B 1 6   ? 25.697  25.673 45.196 1.000 30.003  ? 5   TRP   BBB N   1 ? 
ATOM   2063 C  CA  . TRP   B 1 6   ? 25.304  25.348 46.586 1.000 26.644  ? 5   TRP   BBB CA  1 ? 
ATOM   2064 C  C   . TRP   B 1 6   ? 24.037  26.118 46.934 1.000 28.331  ? 5   TRP   BBB C   1 ? 
ATOM   2065 O  O   . TRP   B 1 6   ? 23.793  27.171 46.354 1.000 31.722  ? 5   TRP   BBB O   1 ? 
ATOM   2066 C  CB  . TRP   B 1 6   ? 26.418  25.598 47.590 1.000 28.470  ? 5   TRP   BBB CB  1 ? 
ATOM   2067 C  CG  . TRP   B 1 6   ? 26.689  27.047 47.842 1.000 28.447  ? 5   TRP   BBB CG  1 ? 
ATOM   2068 C  CD1 . TRP   B 1 6   ? 27.619  27.843 47.228 1.000 29.072  ? 5   TRP   BBB CD1 1 ? 
ATOM   2069 C  CD2 . TRP   B 1 6   ? 26.005  27.873 48.801 1.000 22.217  ? 5   TRP   BBB CD2 1 ? 
ATOM   2070 N  NE1 . TRP   B 1 6   ? 27.536  29.116 47.733 1.000 27.811  ? 5   TRP   BBB NE1 1 ? 
ATOM   2071 C  CE2 . TRP   B 1 6   ? 26.595  29.147 48.735 1.000 24.512  ? 5   TRP   BBB CE2 1 ? 
ATOM   2072 C  CE3 . TRP   B 1 6   ? 24.971  27.637 49.712 1.000 24.788  ? 5   TRP   BBB CE3 1 ? 
ATOM   2073 C  CZ2 . TRP   B 1 6   ? 26.123  30.203 49.522 1.000 25.504  ? 5   TRP   BBB CZ2 1 ? 
ATOM   2074 C  CZ3 . TRP   B 1 6   ? 24.526  28.659 50.514 1.000 24.416  ? 5   TRP   BBB CZ3 1 ? 
ATOM   2075 C  CH2 . TRP   B 1 6   ? 25.133  29.920 50.438 1.000 22.252  ? 5   TRP   BBB CH2 1 ? 
ATOM   2076 N  N   . GLY   B 1 7   ? 23.236  25.554 47.827 1.000 27.149  ? 6   GLY   BBB N   1 ? 
ATOM   2077 C  CA  . GLY   B 1 7   ? 21.930  26.126 48.199 1.000 28.130  ? 6   GLY   BBB CA  1 ? 
ATOM   2078 C  C   . GLY   B 1 7   ? 21.487  25.521 49.511 1.000 26.766  ? 6   GLY   BBB C   1 ? 
ATOM   2079 O  O   . GLY   B 1 7   ? 22.378  25.148 50.307 1.000 24.279  ? 6   GLY   BBB O   1 ? 
ATOM   2080 N  N   . TYR   B 1 8   ? 20.174  25.420 49.706 1.000 28.433  ? 7   TYR   BBB N   1 ? 
ATOM   2081 C  CA  . TYR   B 1 8   ? 19.577  24.856 50.937 1.000 29.783  ? 7   TYR   BBB CA  1 ? 
ATOM   2082 C  C   . TYR   B 1 8   ? 18.596  23.721 50.562 1.000 36.680  ? 7   TYR   BBB C   1 ? 
ATOM   2083 O  O   . TYR   B 1 8   ? 17.895  23.222 51.492 1.000 35.928  ? 7   TYR   BBB O   1 ? 
ATOM   2084 C  CB  . TYR   B 1 8   ? 18.943  25.980 51.762 1.000 28.458  ? 7   TYR   BBB CB  1 ? 
ATOM   2085 C  CG  . TYR   B 1 8   ? 19.989  26.895 52.376 1.000 21.620  ? 7   TYR   BBB CG  1 ? 
ATOM   2086 C  CD1 . TYR   B 1 8   ? 20.573  26.621 53.601 1.000 22.731  ? 7   TYR   BBB CD1 1 ? 
ATOM   2087 C  CD2 . TYR   B 1 8   ? 20.332  28.087 51.761 1.000 21.836  ? 7   TYR   BBB CD2 1 ? 
ATOM   2088 C  CE1 . TYR   B 1 8   ? 21.559  27.404 54.166 1.000 21.753  ? 7   TYR   BBB CE1 1 ? 
ATOM   2089 C  CE2 . TYR   B 1 8   ? 21.274  28.938 52.338 1.000 21.548  ? 7   TYR   BBB CE2 1 ? 
ATOM   2090 C  CZ  . TYR   B 1 8   ? 21.846  28.624 53.556 1.000 21.676  ? 7   TYR   BBB CZ  1 ? 
ATOM   2091 O  OH  . TYR   B 1 8   ? 22.796  29.417 54.115 1.000 20.898  ? 7   TYR   BBB OH  1 ? 
ATOM   2092 N  N   . ASP   B 1 9   ? 18.475  23.398 49.267 1.000 36.292  ? 8   ASP   BBB N   1 ? 
ATOM   2093 C  CA  . ASP   B 1 9   ? 17.500  22.329 48.876 1.000 41.245  ? 8   ASP   BBB CA  1 ? 
ATOM   2094 C  C   . ASP   B 1 9   ? 18.110  20.944 49.168 1.000 41.723  ? 8   ASP   BBB C   1 ? 
ATOM   2095 O  O   . ASP   B 1 9   ? 19.324  20.868 49.462 1.000 33.940  ? 8   ASP   BBB O   1 ? 
ATOM   2096 C  CB  . ASP   B 1 9   ? 16.953  22.526 47.457 1.000 46.808  ? 8   ASP   BBB CB  1 ? 
ATOM   2097 C  CG  . ASP   B 1 9   ? 17.983  22.609 46.344 1.000 58.260  ? 8   ASP   BBB CG  1 ? 
ATOM   2098 O  OD1 . ASP   B 1 9   ? 18.826  21.680 46.229 1.000 58.487  ? 8   ASP   BBB OD1 1 ? 
ATOM   2099 O  OD2 . ASP   B 1 9   ? 17.912  23.586 45.580 1.000 71.576  ? 8   ASP   BBB OD2 1 ? 
ATOM   2100 N  N   . ASP   B 1 10  ? 17.273  19.890 49.106 1.000 45.974  ? 9   ASP   BBB N   1 ? 
ATOM   2101 C  CA  . ASP   B 1 10  ? 17.641  18.468 49.321 1.000 58.553  ? 9   ASP   BBB CA  1 ? 
ATOM   2102 C  C   . ASP   B 1 10  ? 18.219  17.985 47.991 1.000 71.381  ? 9   ASP   BBB C   1 ? 
ATOM   2103 O  O   . ASP   B 1 10  ? 17.422  17.421 47.187 1.000 108.918 ? 9   ASP   BBB O   1 ? 
ATOM   2104 C  CB  . ASP   B 1 10  ? 16.436  17.629 49.785 1.000 59.335  ? 9   ASP   BBB CB  1 ? 
ATOM   2105 N  N   . LYS   B 1 11  ? 19.525  18.245 47.784 1.000 62.591  ? 10  LYS   BBB N   1 ? 
ATOM   2106 C  CA  . LYS   B 1 11  ? 20.252  18.206 46.477 1.000 44.840  ? 10  LYS   BBB CA  1 ? 
ATOM   2107 C  C   . LYS   B 1 11  ? 21.541  19.067 46.515 1.000 44.047  ? 10  LYS   BBB C   1 ? 
ATOM   2108 O  O   . LYS   B 1 11  ? 22.614  18.519 46.157 1.000 44.042  ? 10  LYS   BBB O   1 ? 
ATOM   2109 C  CB  . LYS   B 1 11  ? 19.310  18.625 45.341 1.000 54.785  ? 10  LYS   BBB CB  1 ? 
ATOM   2110 C  CG  . LYS   B 1 11  ? 19.958  18.877 43.986 1.000 68.256  ? 10  LYS   BBB CG  1 ? 
ATOM   2111 C  CD  . LYS   B 1 11  ? 18.955  18.899 42.840 1.000 73.703  ? 10  LYS   BBB CD  1 ? 
ATOM   2112 C  CE  . LYS   B 1 11  ? 19.294  17.930 41.724 1.000 77.779  ? 10  LYS   BBB CE  1 ? 
ATOM   2113 N  NZ  . LYS   B 1 11  ? 20.565  18.280 41.045 1.000 76.740  ? 10  LYS   BBB NZ  1 ? 
ATOM   2114 N  N   . ASN   B 1 12  ? 21.485  20.344 46.925 1.000 38.799  ? 11  ASN   BBB N   1 ? 
ATOM   2115 C  CA  . ASN   B 1 12  ? 22.684  21.246 46.986 1.000 37.669  ? 11  ASN   BBB CA  1 ? 
ATOM   2116 C  C   . ASN   B 1 12  ? 22.848  21.849 48.392 1.000 31.053  ? 11  ASN   BBB C   1 ? 
ATOM   2117 O  O   . ASN   B 1 12  ? 23.697  22.792 48.583 1.000 34.256  ? 11  ASN   BBB O   1 ? 
ATOM   2118 C  CB  . ASN   B 1 12  ? 22.628  22.359 45.930 1.000 35.810  ? 11  ASN   BBB CB  1 ? 
ATOM   2119 C  CG  . ASN   B 1 12  ? 21.521  23.385 46.135 1.000 35.961  ? 11  ASN   BBB CG  1 ? 
ATOM   2120 O  OD1 . ASN   B 1 12  ? 20.791  23.355 47.136 1.000 35.604  ? 11  ASN   BBB OD1 1 ? 
ATOM   2121 N  ND2 . ASN   B 1 12  ? 21.387  24.288 45.171 1.000 37.687  ? 11  ASN   BBB ND2 1 ? 
ATOM   2122 N  N   . GLY   B 1 13  ? 22.099  21.302 49.355 1.000 29.502  ? 12  GLY   BBB N   1 ? 
ATOM   2123 C  CA  . GLY   B 1 13  ? 21.979  21.811 50.731 1.000 31.065  ? 12  GLY   BBB CA  1 ? 
ATOM   2124 C  C   . GLY   B 1 13  ? 23.120  21.409 51.664 1.000 29.523  ? 12  GLY   BBB C   1 ? 
ATOM   2125 O  O   . GLY   B 1 13  ? 24.103  20.749 51.274 1.000 31.541  ? 12  GLY   BBB O   1 ? 
ATOM   2126 N  N   . PRO   B 1 14  ? 22.984  21.832 52.948 1.000 29.177  ? 13  PRO   BBB N   1 ? 
ATOM   2127 C  CA  . PRO   B 1 14  ? 24.006  21.636 53.975 1.000 29.938  ? 13  PRO   BBB CA  1 ? 
ATOM   2128 C  C   . PRO   B 1 14  ? 24.558  20.213 54.043 1.000 30.361  ? 13  PRO   BBB C   1 ? 
ATOM   2129 O  O   . PRO   B 1 14  ? 25.707  20.027 54.315 1.000 29.329  ? 13  PRO   BBB O   1 ? 
ATOM   2130 C  CB  . PRO   B 1 14  ? 23.245  21.945 55.272 1.000 30.115  ? 13  PRO   BBB CB  1 ? 
ATOM   2131 C  CG  . PRO   B 1 14  ? 22.243  23.007 54.847 1.000 26.396  ? 13  PRO   BBB CG  1 ? 
ATOM   2132 C  CD  . PRO   B 1 14  ? 21.847  22.634 53.438 1.000 31.983  ? 13  PRO   BBB CD  1 ? 
ATOM   2133 N  N   . GLU   B 1 15  ? 23.695  19.228 53.829 1.000 36.242  ? 14  GLU   BBB N   1 ? 
ATOM   2134 C  CA  . GLU   B 1 15  ? 24.135  17.809 53.973 1.000 38.940  ? 14  GLU   BBB CA  1 ? 
ATOM   2135 C  C   . GLU   B 1 15  ? 25.079  17.419 52.818 1.000 37.863  ? 14  GLU   BBB C   1 ? 
ATOM   2136 O  O   . GLU   B 1 15  ? 25.889  16.468 53.000 1.000 39.112  ? 14  GLU   BBB O   1 ? 
ATOM   2137 C  CB  . GLU   B 1 15  ? 22.894  16.917 54.106 1.000 38.838  ? 14  GLU   BBB CB  1 ? 
ATOM   2138 C  CG  . GLU   B 1 15  ? 21.988  17.328 55.270 1.000 50.351  ? 14  GLU   BBB CG  1 ? 
ATOM   2139 C  CD  . GLU   B 1 15  ? 22.686  17.596 56.604 1.000 58.722  ? 14  GLU   BBB CD  1 ? 
ATOM   2140 O  OE1 . GLU   B 1 15  ? 22.275  18.557 57.334 1.000 58.204  ? 14  GLU   BBB OE1 1 ? 
ATOM   2141 O  OE2 . GLU   B 1 15  ? 23.639  16.840 56.926 1.000 58.777  ? 14  GLU   BBB OE2 1 ? 
ATOM   2142 N  N   . GLN   B 1 16  ? 24.987  18.119 51.684 1.000 33.050  ? 15  GLN   BBB N   1 ? 
ATOM   2143 C  CA  . GLN   B 1 16  ? 25.768  17.839 50.435 1.000 38.722  ? 15  GLN   BBB CA  1 ? 
ATOM   2144 C  C   . GLN   B 1 16  ? 26.980  18.776 50.354 1.000 32.230  ? 15  GLN   BBB C   1 ? 
ATOM   2145 O  O   . GLN   B 1 16  ? 27.755  18.605 49.410 1.000 31.141  ? 15  GLN   BBB O   1 ? 
ATOM   2146 C  CB  . GLN   B 1 16  ? 24.961  18.091 49.150 1.000 47.597  ? 15  GLN   BBB CB  1 ? 
ATOM   2147 C  CG  . GLN   B 1 16  ? 24.131  16.907 48.690 1.000 68.683  ? 15  GLN   BBB CG  1 ? 
ATOM   2148 C  CD  . GLN   B 1 16  ? 23.011  16.569 49.643 1.000 74.649  ? 15  GLN   BBB CD  1 ? 
ATOM   2149 O  OE1 . GLN   B 1 16  ? 22.036  17.332 49.809 1.000 92.899  ? 15  GLN   BBB OE1 1 ? 
ATOM   2150 N  NE2 . GLN   B 1 16  ? 23.136  15.393 50.254 1.000 62.183  ? 15  GLN   BBB NE2 1 ? 
ATOM   2151 N  N   . TRP   B 1 17  ? 27.061  19.835 51.188 1.000 26.910  ? 16  TRP   BBB N   1 ? 
ATOM   2152 C  CA  . TRP   B 1 17  ? 28.081  20.907 50.965 1.000 24.933  ? 16  TRP   BBB CA  1 ? 
ATOM   2153 C  C   . TRP   B 1 17  ? 29.517  20.346 50.978 1.000 30.282  ? 16  TRP   BBB C   1 ? 
ATOM   2154 O  O   . TRP   B 1 17  ? 30.426  20.931 50.280 1.000 31.372  ? 16  TRP   BBB O   1 ? 
ATOM   2155 C  CB  . TRP   B 1 17  ? 27.967  22.038 51.987 1.000 28.366  ? 16  TRP   BBB CB  1 ? 
ATOM   2156 C  CG  . TRP   B 1 17  ? 26.804  22.951 51.784 1.000 24.581  ? 16  TRP   BBB CG  1 ? 
ATOM   2157 C  CD1 . TRP   B 1 17  ? 26.001  23.087 50.688 1.000 24.504  ? 16  TRP   BBB CD1 1 ? 
ATOM   2158 C  CD2 . TRP   B 1 17  ? 26.366  23.948 52.725 1.000 22.942  ? 16  TRP   BBB CD2 1 ? 
ATOM   2159 N  NE1 . TRP   B 1 17  ? 25.101  24.121 50.894 1.000 24.841  ? 16  TRP   BBB NE1 1 ? 
ATOM   2160 C  CE2 . TRP   B 1 17  ? 25.226  24.560 52.172 1.000 23.536  ? 16  TRP   BBB CE2 1 ? 
ATOM   2161 C  CE3 . TRP   B 1 17  ? 26.730  24.246 54.037 1.000 22.402  ? 16  TRP   BBB CE3 1 ? 
ATOM   2162 C  CZ2 . TRP   B 1 17  ? 24.551  25.606 52.831 1.000 24.785  ? 16  TRP   BBB CZ2 1 ? 
ATOM   2163 C  CZ3 . TRP   B 1 17  ? 26.057  25.267 54.696 1.000 22.686  ? 16  TRP   BBB CZ3 1 ? 
ATOM   2164 C  CH2 . TRP   B 1 17  ? 24.928  25.874 54.126 1.000 24.178  ? 16  TRP   BBB CH2 1 ? 
ATOM   2165 N  N   . SER   B 1 18  ? 29.761  19.300 51.766 1.000 31.823  ? 17  SER   BBB N   1 ? 
ATOM   2166 C  CA  . SER   B 1 18  ? 31.122  18.704 51.923 1.000 33.045  ? 17  SER   BBB CA  1 ? 
ATOM   2167 C  C   . SER   B 1 18  ? 31.720  18.245 50.572 1.000 28.895  ? 17  SER   BBB C   1 ? 
ATOM   2168 O  O   . SER   B 1 18  ? 32.981  18.254 50.459 1.000 31.074  ? 17  SER   BBB O   1 ? 
ATOM   2169 C  CB  . SER   B 1 18  ? 31.095  17.607 52.940 1.000 33.922  ? 17  SER   BBB CB  1 ? 
ATOM   2170 O  OG  . SER   B 1 18  ? 30.416  16.468 52.412 1.000 37.598  ? 17  SER   BBB OG  1 ? 
ATOM   2171 N  N   . LYS   B 1 19  ? 30.888  17.972 49.551 1.000 29.497  ? 18  LYS   BBB N   1 ? 
ATOM   2172 C  CA  . LYS   B 1 19  ? 31.382  17.523 48.203 1.000 33.221  ? 18  LYS   BBB CA  1 ? 
ATOM   2173 C  C   . LYS   B 1 19  ? 32.205  18.650 47.557 1.000 39.115  ? 18  LYS   BBB C   1 ? 
ATOM   2174 O  O   . LYS   B 1 19  ? 33.359  18.391 47.118 1.000 33.041  ? 18  LYS   BBB O   1 ? 
ATOM   2175 C  CB  . LYS   B 1 19  ? 30.231  17.014 47.321 1.000 33.042  ? 18  LYS   BBB CB  1 ? 
ATOM   2176 C  CG  . LYS   B 1 19  ? 29.520  15.785 47.906 1.000 40.545  ? 18  LYS   BBB CG  1 ? 
ATOM   2177 C  CD  . LYS   B 1 19  ? 28.568  15.045 46.971 1.000 56.945  ? 18  LYS   BBB CD  1 ? 
ATOM   2178 C  CE  . LYS   B 1 19  ? 27.388  15.891 46.535 1.000 58.019  ? 18  LYS   BBB CE  1 ? 
ATOM   2179 N  NZ  . LYS   B 1 19  ? 26.095  15.182 46.685 1.000 70.840  ? 18  LYS   BBB NZ  1 ? 
ATOM   2180 N  N   . LEU   B 1 20  ? 31.674  19.885 47.575 1.000 32.814  ? 19  LEU   BBB N   1 ? 
ATOM   2181 C  CA  . LEU   B 1 20  ? 32.338  21.067 46.943 1.000 29.705  ? 19  LEU   BBB CA  1 ? 
ATOM   2182 C  C   . LEU   B 1 20  ? 33.239  21.777 47.984 1.000 24.710  ? 19  LEU   BBB C   1 ? 
ATOM   2183 O  O   . LEU   B 1 20  ? 34.221  22.445 47.579 1.000 36.274  ? 19  LEU   BBB O   1 ? 
ATOM   2184 C  CB  . LEU   B 1 20  ? 31.252  22.004 46.394 1.000 36.954  ? 19  LEU   BBB CB  1 ? 
ATOM   2185 C  CG  . LEU   B 1 20  ? 30.745  21.725 44.975 1.000 45.277  ? 19  LEU   BBB CG  1 ? 
ATOM   2186 C  CD1 . LEU   B 1 20  ? 30.654  20.238 44.680 1.000 56.755  ? 19  LEU   BBB CD1 1 ? 
ATOM   2187 C  CD2 . LEU   B 1 20  ? 29.392  22.391 44.748 1.000 43.567  ? 19  LEU   BBB CD2 1 ? 
ATOM   2188 N  N   . TYR   B 1 21  ? 32.928  21.619 49.275 1.000 26.365  ? 20  TYR   BBB N   1 ? 
ATOM   2189 C  CA  . TYR   B 1 21  ? 33.575  22.341 50.401 1.000 25.352  ? 20  TYR   BBB CA  1 ? 
ATOM   2190 C  C   . TYR   B 1 21  ? 33.837  21.345 51.524 1.000 30.057  ? 20  TYR   BBB C   1 ? 
ATOM   2191 O  O   . TYR   B 1 21  ? 33.050  21.324 52.501 1.000 30.430  ? 20  TYR   BBB O   1 ? 
ATOM   2192 C  CB  . TYR   B 1 21  ? 32.678  23.498 50.863 1.000 29.552  ? 20  TYR   BBB CB  1 ? 
ATOM   2193 C  CG  . TYR   B 1 21  ? 32.356  24.485 49.751 1.000 28.378  ? 20  TYR   BBB CG  1 ? 
ATOM   2194 C  CD1 . TYR   B 1 21  ? 33.269  25.460 49.372 1.000 31.555  ? 20  TYR   BBB CD1 1 ? 
ATOM   2195 C  CD2 . TYR   B 1 21  ? 31.206  24.357 48.982 1.000 29.073  ? 20  TYR   BBB CD2 1 ? 
ATOM   2196 C  CE1 . TYR   B 1 21  ? 33.046  26.271 48.266 1.000 35.002  ? 20  TYR   BBB CE1 1 ? 
ATOM   2197 C  CE2 . TYR   B 1 21  ? 30.939  25.192 47.900 1.000 32.629  ? 20  TYR   BBB CE2 1 ? 
ATOM   2198 C  CZ  . TYR   B 1 21  ? 31.878  26.139 47.526 1.000 31.839  ? 20  TYR   BBB CZ  1 ? 
ATOM   2199 O  OH  . TYR   B 1 21  ? 31.639  26.954 46.447 1.000 37.627  ? 20  TYR   BBB OH  1 ? 
ATOM   2200 N  N   . PRO   B 1 22  ? 34.951  20.592 51.413 1.000 35.242  ? 21  PRO   BBB N   1 ? 
ATOM   2201 C  CA  . PRO   B 1 22  ? 35.259  19.531 52.379 1.000 32.546  ? 21  PRO   BBB CA  1 ? 
ATOM   2202 C  C   . PRO   B 1 22  ? 35.502  20.025 53.815 1.000 31.012  ? 21  PRO   BBB C   1 ? 
ATOM   2203 O  O   . PRO   B 1 22  ? 35.310  19.258 54.747 1.000 30.186  ? 21  PRO   BBB O   1 ? 
ATOM   2204 C  CB  . PRO   B 1 22  ? 36.557  18.968 51.797 1.000 35.385  ? 21  PRO   BBB CB  1 ? 
ATOM   2205 C  CG  . PRO   B 1 22  ? 36.393  19.222 50.321 1.000 39.627  ? 21  PRO   BBB CG  1 ? 
ATOM   2206 C  CD  . PRO   B 1 22  ? 35.881  20.641 50.287 1.000 36.043  ? 21  PRO   BBB CD  1 ? 
ATOM   2207 N  N   . ILE   B 1 23  ? 35.835  21.326 53.962 1.000 30.544  ? 22  ILE   BBB N   1 ? 
ATOM   2208 C  CA  . ILE   B 1 23  ? 35.907  22.009 55.310 1.000 26.954  ? 22  ILE   BBB CA  1 ? 
ATOM   2209 C  C   . ILE   B 1 23  ? 34.518  22.029 56.041 1.000 26.645  ? 22  ILE   BBB C   1 ? 
ATOM   2210 O  O   . ILE   B 1 23  ? 34.520  22.329 57.304 1.000 31.917  ? 22  ILE   BBB O   1 ? 
ATOM   2211 C  CB  . ILE   B 1 23  ? 36.463  23.444 55.224 1.000 24.867  ? 22  ILE   BBB CB  1 ? 
ATOM   2212 C  CG1 . ILE   B 1 23  ? 37.019  23.894 56.581 1.000 30.565  ? 22  ILE   BBB CG1 1 ? 
ATOM   2213 C  CG2 . ILE   B 1 23  ? 35.395  24.402 54.700 1.000 28.037  ? 22  ILE   BBB CG2 1 ? 
ATOM   2214 C  CD1 . ILE   B 1 23  ? 38.131  23.015 57.117 1.000 38.920  ? 22  ILE   BBB CD1 1 ? 
ATOM   2215 N  N   . ALA   B 1 24  ? 33.420  21.681 55.334 1.000 26.799  ? 23  ALA   BBB N   1 ? 
ATOM   2216 C  CA  . ALA   B 1 24  ? 32.072  21.482 55.943 1.000 28.919  ? 23  ALA   BBB CA  1 ? 
ATOM   2217 C  C   . ALA   B 1 24  ? 32.160  20.452 57.083 1.000 31.566  ? 23  ALA   BBB C   1 ? 
ATOM   2218 O  O   . ALA   B 1 24  ? 31.358  20.550 58.020 1.000 29.319  ? 23  ALA   BBB O   1 ? 
ATOM   2219 C  CB  . ALA   B 1 24  ? 31.062  21.032 54.896 1.000 32.060  ? 23  ALA   BBB CB  1 ? 
ATOM   2220 N  N   . ASN   B 1 25  ? 33.077  19.458 56.986 1.000 32.404  ? 24  ASN   BBB N   1 ? 
ATOM   2221 C  CA  . ASN   B 1 25  ? 33.287  18.450 58.059 1.000 28.247  ? 24  ASN   BBB CA  1 ? 
ATOM   2222 C  C   . ASN   B 1 25  ? 34.445  18.825 59.003 1.000 28.189  ? 24  ASN   BBB C   1 ? 
ATOM   2223 O  O   . ASN   B 1 25  ? 34.933  17.936 59.740 1.000 30.837  ? 24  ASN   BBB O   1 ? 
ATOM   2224 C  CB  . ASN   B 1 25  ? 33.531  17.045 57.452 1.000 34.010  ? 24  ASN   BBB CB  1 ? 
ATOM   2225 C  CG  . ASN   B 1 25  ? 32.334  16.543 56.630 1.000 36.142  ? 24  ASN   BBB CG  1 ? 
ATOM   2226 O  OD1 . ASN   B 1 25  ? 32.469  16.051 55.408 1.000 45.233  ? 24  ASN   BBB OD1 1 ? 
ATOM   2227 N  ND2 . ASN   B 1 25  ? 31.145  16.651 57.272 1.000 37.809  ? 24  ASN   BBB ND2 1 ? 
ATOM   2228 N  N   . GLY   B 1 26  ? 34.883  20.084 59.030 1.000 29.929  ? 25  GLY   BBB N   1 ? 
ATOM   2229 C  CA  . GLY   B 1 26  ? 35.999  20.547 59.880 1.000 30.261  ? 25  GLY   BBB CA  1 ? 
ATOM   2230 C  C   . GLY   B 1 26  ? 35.663  20.497 61.386 1.000 31.329  ? 25  GLY   BBB C   1 ? 
ATOM   2231 O  O   . GLY   B 1 26  ? 34.540  20.241 61.799 1.000 31.278  ? 25  GLY   BBB O   1 ? 
ATOM   2232 N  N   . ASN   B 1 27  ? 36.682  20.955 62.169 1.000 31.245  ? 26  ASN   BBB N   1 ? 
ATOM   2233 C  CA  . ASN   B 1 27  ? 36.668  20.964 63.658 1.000 32.420  ? 26  ASN   BBB CA  1 ? 
ATOM   2234 C  C   . ASN   B 1 27  ? 36.158  22.308 64.211 1.000 25.554  ? 26  ASN   BBB C   1 ? 
ATOM   2235 O  O   . ASN   B 1 27  ? 35.935  22.417 65.441 1.000 31.878  ? 26  ASN   BBB O   1 ? 
ATOM   2236 C  CB  . ASN   B 1 27  ? 38.071  20.659 64.185 1.000 36.001  ? 26  ASN   BBB CB  1 ? 
ATOM   2237 C  CG  . ASN   B 1 27  ? 38.480  19.241 63.843 1.000 33.503  ? 26  ASN   BBB CG  1 ? 
ATOM   2238 O  OD1 . ASN   B 1 27  ? 37.619  18.364 63.736 1.000 38.618  ? 26  ASN   BBB OD1 1 ? 
ATOM   2239 N  ND2 . ASN   B 1 27  ? 39.763  19.016 63.607 1.000 41.469  ? 26  ASN   BBB ND2 1 ? 
ATOM   2240 N  N   . ASN   B 1 28  ? 35.958  23.310 63.369 1.000 26.815  ? 27  ASN   BBB N   1 ? 
ATOM   2241 C  CA  . ASN   B 1 28  ? 35.541  24.645 63.862 1.000 25.049  ? 27  ASN   BBB CA  1 ? 
ATOM   2242 C  C   . ASN   B 1 28  ? 34.352  25.107 63.047 1.000 24.604  ? 27  ASN   BBB C   1 ? 
ATOM   2243 O  O   . ASN   B 1 28  ? 34.320  26.325 62.705 1.000 24.383  ? 27  ASN   BBB O   1 ? 
ATOM   2244 C  CB  . ASN   B 1 28  ? 36.690  25.644 63.798 1.000 26.933  ? 27  ASN   BBB CB  1 ? 
ATOM   2245 C  CG  . ASN   B 1 28  ? 37.886  25.227 64.622 1.000 30.736  ? 27  ASN   BBB CG  1 ? 
ATOM   2246 O  OD1 . ASN   B 1 28  ? 38.817  24.621 64.106 1.000 44.908  ? 27  ASN   BBB OD1 1 ? 
ATOM   2247 N  ND2 . ASN   B 1 28  ? 37.871  25.550 65.896 1.000 39.348  ? 27  ASN   BBB ND2 1 ? 
ATOM   2248 N  N   . GLN   B 1 29  ? 33.355  24.276 62.843 1.000 23.170  ? 28  GLN   BBB N   1 ? 
ATOM   2249 C  CA  . GLN   B 1 29  ? 32.200  24.622 61.969 1.000 23.386  ? 28  GLN   BBB CA  1 ? 
ATOM   2250 C  C   . GLN   B 1 29  ? 31.084  25.266 62.800 1.000 23.113  ? 28  GLN   BBB C   1 ? 
ATOM   2251 O  O   . GLN   B 1 29  ? 30.999  25.050 64.034 1.000 24.365  ? 28  GLN   BBB O   1 ? 
ATOM   2252 C  CB  . GLN   B 1 29  ? 31.743  23.344 61.249 1.000 22.402  ? 28  GLN   BBB CB  1 ? 
ATOM   2253 C  CG  . GLN   B 1 29  ? 32.644  22.994 60.052 1.000 25.479  ? 28  GLN   BBB CG  1 ? 
ATOM   2254 C  CD  . GLN   B 1 29  ? 32.656  24.090 58.990 1.000 23.429  ? 28  GLN   BBB CD  1 ? 
ATOM   2255 O  OE1 . GLN   B 1 29  ? 31.675  24.254 58.215 1.000 23.803  ? 28  GLN   BBB OE1 1 ? 
ATOM   2256 N  NE2 . GLN   B 1 29  ? 33.831  24.718 58.847 1.000 25.457  ? 28  GLN   BBB NE2 1 ? 
ATOM   2257 N  N   . SER   B 1 30  ? 30.354  26.219 62.166 1.000 23.365  ? 29  SER   BBB N   1 ? 
ATOM   2258 C  CA  . SER   B 1 30  ? 29.225  26.917 62.802 1.000 21.774  ? 29  SER   BBB CA  1 ? 
ATOM   2259 C  C   . SER   B 1 30  ? 27.964  26.704 61.952 1.000 25.682  ? 29  SER   BBB C   1 ? 
ATOM   2260 O  O   . SER   B 1 30  ? 28.068  26.526 60.740 1.000 23.489  ? 29  SER   BBB O   1 ? 
ATOM   2261 C  CB  . SER   B 1 30  ? 29.560  28.410 62.836 1.000 23.079  ? 29  SER   BBB CB  1 ? 
ATOM   2262 O  OG  . SER   B 1 30  ? 30.685  28.633 63.659 1.000 22.396  ? 29  SER   BBB OG  1 ? 
ATOM   2263 N  N   . PRO   B 1 31  ? 26.752  26.899 62.506 1.000 24.326  ? 30  PRO   BBB N   1 ? 
ATOM   2264 C  CA  . PRO   B 1 31  ? 26.532  27.302 63.901 1.000 21.152  ? 30  PRO   BBB CA  1 ? 
ATOM   2265 C  C   . PRO   B 1 31  ? 26.709  26.117 64.864 1.000 19.248  ? 30  PRO   BBB C   1 ? 
ATOM   2266 O  O   . PRO   B 1 31  ? 26.992  24.954 64.405 1.000 22.711  ? 30  PRO   BBB O   1 ? 
ATOM   2267 C  CB  . PRO   B 1 31  ? 25.059  27.781 63.867 1.000 19.577  ? 30  PRO   BBB CB  1 ? 
ATOM   2268 C  CG  . PRO   B 1 31  ? 24.436  26.813 62.853 1.000 23.985  ? 30  PRO   BBB CG  1 ? 
ATOM   2269 C  CD  . PRO   B 1 31  ? 25.489  26.685 61.783 1.000 24.389  ? 30  PRO   BBB CD  1 ? 
ATOM   2270 N  N   . VAL   B 1 32  ? 26.558  26.389 66.156 1.000 20.991  ? 31  VAL   BBB N   1 ? 
ATOM   2271 C  CA  . VAL   B 1 32  ? 26.614  25.351 67.242 1.000 21.871  ? 31  VAL   BBB CA  1 ? 
ATOM   2272 C  C   . VAL   B 1 32  ? 25.445  25.572 68.181 1.000 21.512  ? 31  VAL   BBB C   1 ? 
ATOM   2273 O  O   . VAL   B 1 32  ? 24.819  26.678 68.186 1.000 23.267  ? 31  VAL   BBB O   1 ? 
ATOM   2274 C  CB  . VAL   B 1 32  ? 27.942  25.399 68.000 1.000 24.118  ? 31  VAL   BBB CB  1 ? 
ATOM   2275 C  CG1 . VAL   B 1 32  ? 29.091  25.196 67.023 1.000 27.418  ? 31  VAL   BBB CG1 1 ? 
ATOM   2276 C  CG2 . VAL   B 1 32  ? 28.101  26.720 68.765 1.000 25.058  ? 31  VAL   BBB CG2 1 ? 
ATOM   2277 N  N   . ASP   B 1 33  ? 25.067  24.558 68.917 1.000 26.860  ? 32  ASP   BBB N   1 ? 
ATOM   2278 C  CA  . ASP   B 1 33  ? 24.196  24.656 70.089 1.000 27.954  ? 32  ASP   BBB CA  1 ? 
ATOM   2279 C  C   . ASP   B 1 33  ? 25.057  25.134 71.266 1.000 23.120  ? 32  ASP   BBB C   1 ? 
ATOM   2280 O  O   . ASP   B 1 33  ? 26.190  24.621 71.495 1.000 27.250  ? 32  ASP   BBB O   1 ? 
ATOM   2281 C  CB  . ASP   B 1 33  ? 23.573  23.316 70.499 1.000 27.026  ? 32  ASP   BBB CB  1 ? 
ATOM   2282 C  CG  . ASP   B 1 33  ? 22.664  23.466 71.708 1.000 25.367  ? 32  ASP   BBB CG  1 ? 
ATOM   2283 O  OD1 . ASP   B 1 33  ? 21.715  24.333 71.673 1.000 23.863  ? 32  ASP   BBB OD1 1 ? 
ATOM   2284 O  OD2 . ASP   B 1 33  ? 22.933  22.878 72.741 1.000 30.705  ? 32  ASP   BBB OD2 1 ? 
ATOM   2285 N  N   . ILE   B 1 34  ? 24.565  26.164 71.960 1.000 26.399  ? 33  ILE   BBB N   1 ? 
ATOM   2286 C  CA  . ILE   B 1 34  ? 25.222  26.611 73.212 1.000 23.226  ? 33  ILE   BBB CA  1 ? 
ATOM   2287 C  C   . ILE   B 1 34  ? 24.545  25.978 74.414 1.000 22.747  ? 33  ILE   BBB C   1 ? 
ATOM   2288 O  O   . ILE   B 1 34  ? 23.362  26.330 74.698 1.000 22.133  ? 33  ILE   BBB O   1 ? 
ATOM   2289 C  CB  . ILE   B 1 34  ? 25.145  28.144 73.289 1.000 22.337  ? 33  ILE   BBB CB  1 ? 
ATOM   2290 C  CG1 . ILE   B 1 34  ? 25.798  28.739 72.046 1.000 24.002  ? 33  ILE   BBB CG1 1 ? 
ATOM   2291 C  CG2 . ILE   B 1 34  ? 25.761  28.630 74.588 1.000 22.921  ? 33  ILE   BBB CG2 1 ? 
ATOM   2292 C  CD1 . ILE   B 1 34  ? 25.783  30.236 72.020 1.000 23.361  ? 33  ILE   BBB CD1 1 ? 
ATOM   2293 N  N   . LYS   B 1 35  ? 25.234  24.995 75.022 1.000 24.052  ? 34  LYS   BBB N   1 ? 
ATOM   2294 C  CA  . LYS   B 1 35  ? 24.728  24.349 76.242 1.000 25.020  ? 34  LYS   BBB CA  1 ? 
ATOM   2295 C  C   . LYS   B 1 35  ? 25.176  25.215 77.429 1.000 26.043  ? 34  LYS   BBB C   1 ? 
ATOM   2296 O  O   . LYS   B 1 35  ? 26.390  25.247 77.726 1.000 24.172  ? 34  LYS   BBB O   1 ? 
ATOM   2297 C  CB  . LYS   B 1 35  ? 25.174  22.872 76.288 1.000 28.444  ? 34  LYS   BBB CB  1 ? 
ATOM   2298 C  CG  . LYS   B 1 35  ? 24.781  22.173 77.561 1.000 36.578  ? 34  LYS   BBB CG  1 ? 
ATOM   2299 C  CD  . LYS   B 1 35  ? 24.794  20.670 77.435 1.000 53.417  ? 34  LYS   BBB CD  1 ? 
ATOM   2300 C  CE  . LYS   B 1 35  ? 23.894  19.982 78.443 1.000 67.380  ? 34  LYS   BBB CE  1 ? 
ATOM   2301 N  NZ  . LYS   B 1 35  ? 24.251  18.552 78.600 1.000 76.090  ? 34  LYS   BBB NZ  1 ? 
ATOM   2302 N  N   . THR   B 1 36  ? 24.237  25.958 78.048 1.000 25.212  ? 35  THR   BBB N   1 ? 
ATOM   2303 C  CA  . THR   B 1 36  ? 24.611  27.015 79.046 1.000 25.752  ? 35  THR   BBB CA  1 ? 
ATOM   2304 C  C   . THR   B 1 36  ? 25.270  26.356 80.271 1.000 31.025  ? 35  THR   BBB C   1 ? 
ATOM   2305 O  O   . THR   B 1 36  ? 26.128  26.969 80.863 1.000 32.942  ? 35  THR   BBB O   1 ? 
ATOM   2306 C  CB  . THR   B 1 36  ? 23.406  27.888 79.403 1.000 26.186  ? 35  THR   BBB CB  1 ? 
ATOM   2307 O  OG1 . THR   B 1 36  ? 22.347  27.066 79.883 1.000 28.477  ? 35  THR   BBB OG1 1 ? 
ATOM   2308 C  CG2 . THR   B 1 36  ? 22.889  28.639 78.199 1.000 29.517  ? 35  THR   BBB CG2 1 ? 
ATOM   2309 N  N   . SER   B 1 37  ? 24.970  25.087 80.582 1.000 31.305  ? 36  SER   BBB N   1 ? 
ATOM   2310 C  CA  . SER   B 1 37  ? 25.631  24.393 81.723 1.000 34.917  ? 36  SER   BBB CA  1 ? 
ATOM   2311 C  C   . SER   B 1 37  ? 27.139  24.155 81.467 1.000 31.445  ? 36  SER   BBB C   1 ? 
ATOM   2312 O  O   . SER   B 1 37  ? 27.832  23.861 82.421 1.000 33.857  ? 36  SER   BBB O   1 ? 
ATOM   2313 C  CB  . SER   B 1 37  ? 24.941  23.080 82.040 1.000 36.347  ? 36  SER   BBB CB  1 ? 
ATOM   2314 O  OG  . SER   B 1 37  ? 25.017  22.220 80.907 1.000 35.366  ? 36  SER   BBB OG  1 ? 
ATOM   2315 N  N   . GLU   B 1 38  ? 27.597  24.148 80.213 1.000 26.131  ? 37  GLU   BBB N   1 ? 
ATOM   2316 C  CA  . GLU   B 1 38  ? 29.006  23.835 79.823 1.000 33.262  ? 37  GLU   BBB CA  1 ? 
ATOM   2317 C  C   . GLU   B 1 38  ? 29.781  25.122 79.472 1.000 31.747  ? 37  GLU   BBB C   1 ? 
ATOM   2318 O  O   . GLU   B 1 38  ? 31.015  25.012 79.146 1.000 32.769  ? 37  GLU   BBB O   1 ? 
ATOM   2319 C  CB  . GLU   B 1 38  ? 29.015  22.889 78.616 1.000 34.665  ? 37  GLU   BBB CB  1 ? 
ATOM   2320 C  CG  . GLU   B 1 38  ? 28.211  21.605 78.806 1.000 43.226  ? 37  GLU   BBB CG  1 ? 
ATOM   2321 C  CD  . GLU   B 1 38  ? 28.576  20.802 80.039 1.000 52.484  ? 37  GLU   BBB CD  1 ? 
ATOM   2322 O  OE1 . GLU   B 1 38  ? 29.784  20.550 80.239 1.000 58.715  ? 37  GLU   BBB OE1 1 ? 
ATOM   2323 O  OE2 . GLU   B 1 38  ? 27.652  20.441 80.794 1.000 74.223  ? 37  GLU   BBB OE2 1 ? 
ATOM   2324 N  N   . THR   B 1 39  ? 29.121  26.296 79.498 1.000 24.898  ? 38  THR   BBB N   1 ? 
ATOM   2325 C  CA  . THR   B 1 39  ? 29.826  27.572 79.200 1.000 24.193  ? 38  THR   BBB CA  1 ? 
ATOM   2326 C  C   . THR   B 1 39  ? 30.809  27.873 80.329 1.000 25.380  ? 38  THR   BBB C   1 ? 
ATOM   2327 O  O   . THR   B 1 39  ? 30.527  27.542 81.459 1.000 30.860  ? 38  THR   BBB O   1 ? 
ATOM   2328 C  CB  . THR   B 1 39  ? 28.886  28.762 78.956 1.000 25.704  ? 38  THR   BBB CB  1 ? 
ATOM   2329 O  OG1 . THR   B 1 39  ? 28.022  28.912 80.072 1.000 23.976  ? 38  THR   BBB OG1 1 ? 
ATOM   2330 C  CG2 . THR   B 1 39  ? 28.058  28.582 77.708 1.000 26.989  ? 38  THR   BBB CG2 1 ? 
ATOM   2331 N  N   . LYS   B 1 40  ? 31.902  28.563 80.020 1.000 24.611  ? 39  LYS   BBB N   1 ? 
ATOM   2332 C  CA  . LYS   B 1 40  ? 32.903  28.994 81.021 1.000 28.482  ? 39  LYS   BBB CA  1 ? 
ATOM   2333 C  C   . LYS   B 1 40  ? 32.926  30.540 81.040 1.000 22.373  ? 39  LYS   BBB C   1 ? 
ATOM   2334 O  O   . LYS   B 1 40  ? 32.985  31.160 79.965 1.000 22.634  ? 39  LYS   BBB O   1 ? 
ATOM   2335 C  CB  . LYS   B 1 40  ? 34.264  28.416 80.652 1.000 32.379  ? 39  LYS   BBB CB  1 ? 
ATOM   2336 C  CG  . LYS   B 1 40  ? 34.271  26.897 80.580 1.000 32.289  ? 39  LYS   BBB CG  1 ? 
ATOM   2337 C  CD  . LYS   B 1 40  ? 33.993  26.265 81.918 1.000 36.168  ? 39  LYS   BBB CD  1 ? 
ATOM   2338 C  CE  . LYS   B 1 40  ? 34.129  24.760 81.913 1.000 43.433  ? 39  LYS   BBB CE  1 ? 
ATOM   2339 N  NZ  . LYS   B 1 40  ? 33.596  24.289 83.208 1.000 47.382  ? 39  LYS   BBB NZ  1 ? 
ATOM   2340 N  N   . HIS   B 1 41  ? 32.838  31.115 82.224 1.000 24.576  ? 40  HIS   BBB N   1 ? 
ATOM   2341 C  CA  . HIS   B 1 41  ? 33.006  32.589 82.388 1.000 21.795  ? 40  HIS   BBB CA  1 ? 
ATOM   2342 C  C   . HIS   B 1 41  ? 34.491  32.962 82.271 1.000 25.496  ? 40  HIS   BBB C   1 ? 
ATOM   2343 O  O   . HIS   B 1 41  ? 35.360  32.416 83.020 1.000 25.345  ? 40  HIS   BBB O   1 ? 
ATOM   2344 C  CB  . HIS   B 1 41  ? 32.437  33.123 83.701 1.000 22.345  ? 40  HIS   BBB CB  1 ? 
ATOM   2345 C  CG  . HIS   B 1 41  ? 32.664  34.590 83.803 1.000 24.218  ? 40  HIS   BBB CG  1 ? 
ATOM   2346 N  ND1 . HIS   B 1 41  ? 33.650  35.145 84.577 1.000 25.429  ? 40  HIS   BBB ND1 1 ? 
ATOM   2347 C  CD2 . HIS   B 1 41  ? 32.062  35.607 83.153 1.000 23.185  ? 40  HIS   BBB CD2 1 ? 
ATOM   2348 C  CE1 . HIS   B 1 41  ? 33.635  36.468 84.422 1.000 25.653  ? 40  HIS   BBB CE1 1 ? 
ATOM   2349 N  NE2 . HIS   B 1 41  ? 32.669  36.770 83.544 1.000 26.830  ? 40  HIS   BBB NE2 1 ? 
ATOM   2350 N  N   . ASP   B 1 42  ? 34.786  33.886 81.365 1.000 21.797  ? 41  ASP   BBB N   1 ? 
ATOM   2351 C  CA  . ASP   B 1 42  ? 36.178  34.345 81.126 1.000 25.344  ? 41  ASP   BBB CA  1 ? 
ATOM   2352 C  C   . ASP   B 1 42  ? 36.303  35.820 81.530 1.000 24.117  ? 41  ASP   BBB C   1 ? 
ATOM   2353 O  O   . ASP   B 1 42  ? 35.686  36.658 80.858 1.000 25.315  ? 41  ASP   BBB O   1 ? 
ATOM   2354 C  CB  . ASP   B 1 42  ? 36.527  34.084 79.671 1.000 24.047  ? 41  ASP   BBB CB  1 ? 
ATOM   2355 C  CG  . ASP   B 1 42  ? 37.897  34.527 79.232 1.000 25.343  ? 41  ASP   BBB CG  1 ? 
ATOM   2356 O  OD1 . ASP   B 1 42  ? 38.560  35.222 80.035 1.000 30.402  ? 41  ASP   BBB OD1 1 ? 
ATOM   2357 O  OD2 . ASP   B 1 42  ? 38.280  34.152 78.078 1.000 32.206  ? 41  ASP   BBB OD2 1 ? 
ATOM   2358 N  N   . THR   B 1 43  ? 37.098  36.111 82.561 1.000 20.960  ? 42  THR   BBB N   1 ? 
ATOM   2359 C  CA  . THR   B 1 43  ? 37.220  37.464 83.156 1.000 22.799  ? 42  THR   BBB CA  1 ? 
ATOM   2360 C  C   . THR   B 1 43  ? 37.961  38.373 82.187 1.000 20.666  ? 42  THR   BBB C   1 ? 
ATOM   2361 O  O   . THR   B 1 43  ? 37.843  39.622 82.390 1.000 22.010  ? 42  THR   BBB O   1 ? 
ATOM   2362 C  CB  . THR   B 1 43  ? 37.925  37.432 84.514 1.000 24.035  ? 42  THR   BBB CB  1 ? 
ATOM   2363 O  OG1 . THR   B 1 43  ? 39.298  37.117 84.286 1.000 22.060  ? 42  THR   BBB OG1 1 ? 
ATOM   2364 C  CG2 . THR   B 1 43  ? 37.275  36.465 85.490 1.000 24.718  ? 42  THR   BBB CG2 1 ? 
ATOM   2365 N  N   . SER   B 1 44  ? 38.612  37.842 81.167 1.000 22.143  ? 43  SER   BBB N   1 ? 
ATOM   2366 C  CA  . SER   B 1 44  ? 39.361  38.605 80.141 1.000 23.602  ? 43  SER   BBB CA  1 ? 
ATOM   2367 C  C   . SER   B 1 44  ? 38.412  39.194 79.090 1.000 23.935  ? 43  SER   BBB C   1 ? 
ATOM   2368 O  O   . SER   B 1 44  ? 38.876  40.020 78.312 1.000 24.365  ? 43  SER   BBB O   1 ? 
ATOM   2369 C  CB  . SER   B 1 44  ? 40.487  37.802 79.528 1.000 28.627  ? 43  SER   BBB CB  1 ? 
ATOM   2370 O  OG  . SER   B 1 44  ? 40.025  36.857 78.581 1.000 25.794  ? 43  SER   BBB OG  1 ? 
ATOM   2371 N  N   . LEU   B 1 45  ? 37.131  38.805 79.066 1.000 21.233  ? 44  LEU   BBB N   1 ? 
ATOM   2372 C  CA  . LEU   B 1 45  ? 36.155  39.329 78.062 1.000 21.929  ? 44  LEU   BBB CA  1 ? 
ATOM   2373 C  C   . LEU   B 1 45  ? 35.674  40.743 78.447 1.000 23.372  ? 44  LEU   BBB C   1 ? 
ATOM   2374 O  O   . LEU   B 1 45  ? 34.897  40.918 79.420 1.000 27.981  ? 44  LEU   BBB O   1 ? 
ATOM   2375 C  CB  . LEU   B 1 45  ? 34.979  38.372 77.876 1.000 24.707  ? 44  LEU   BBB CB  1 ? 
ATOM   2376 C  CG  . LEU   B 1 45  ? 35.329  37.043 77.217 1.000 24.649  ? 44  LEU   BBB CG  1 ? 
ATOM   2377 C  CD1 . LEU   B 1 45  ? 34.134  36.104 77.245 1.000 25.117  ? 44  LEU   BBB CD1 1 ? 
ATOM   2378 C  CD2 . LEU   B 1 45  ? 35.804  37.257 75.794 1.000 26.221  ? 44  LEU   BBB CD2 1 ? 
ATOM   2379 N  N   . LYS   B 1 46  ? 36.092  41.726 77.665 1.000 25.556  ? 45  LYS   BBB N   1 ? 
ATOM   2380 C  CA  . LYS   B 1 46  ? 35.571  43.098 77.867 1.000 24.827  ? 45  LYS   BBB CA  1 ? 
ATOM   2381 C  C   . LYS   B 1 46  ? 34.165  43.184 77.310 1.000 24.071  ? 45  LYS   BBB C   1 ? 
ATOM   2382 O  O   . LYS   B 1 46  ? 33.732  42.378 76.497 1.000 23.135  ? 45  LYS   BBB O   1 ? 
ATOM   2383 C  CB  . LYS   B 1 46  ? 36.423  44.172 77.180 1.000 28.797  ? 45  LYS   BBB CB  1 ? 
ATOM   2384 C  CG  . LYS   B 1 46  ? 37.789  44.381 77.790 1.000 30.005  ? 45  LYS   BBB CG  1 ? 
ATOM   2385 C  CD  . LYS   B 1 46  ? 38.510  45.474 77.092 1.000 30.245  ? 45  LYS   BBB CD  1 ? 
ATOM   2386 C  CE  . LYS   B 1 46  ? 39.866  45.736 77.678 1.000 39.634  ? 45  LYS   BBB CE  1 ? 
ATOM   2387 N  NZ  . LYS   B 1 46  ? 40.514  46.887 76.996 1.000 41.544  ? 45  LYS   BBB NZ  1 ? 
ATOM   2388 N  N   . PRO   B 1 47  ? 33.396  44.219 77.691 1.000 25.765  ? 46  PRO   BBB N   1 ? 
ATOM   2389 C  CA  . PRO   B 1 47  ? 32.158  44.492 76.979 1.000 23.569  ? 46  PRO   BBB CA  1 ? 
ATOM   2390 C  C   . PRO   B 1 47  ? 32.440  44.727 75.483 1.000 22.591  ? 46  PRO   BBB C   1 ? 
ATOM   2391 O  O   . PRO   B 1 47  ? 33.565  45.177 75.134 1.000 25.361  ? 46  PRO   BBB O   1 ? 
ATOM   2392 C  CB  . PRO   B 1 47  ? 31.582  45.706 77.698 1.000 25.444  ? 46  PRO   BBB CB  1 ? 
ATOM   2393 C  CG  . PRO   B 1 47  ? 32.305  45.771 79.021 1.000 27.802  ? 46  PRO   BBB CG  1 ? 
ATOM   2394 C  CD  . PRO   B 1 47  ? 33.674  45.169 78.777 1.000 29.991  ? 46  PRO   BBB CD  1 ? 
ATOM   2395 N  N   . ILE   B 1 48  ? 31.438  44.446 74.642 1.000 24.039  ? 47  ILE   BBB N   1 ? 
ATOM   2396 C  CA  . ILE   B 1 48  ? 31.436  44.707 73.179 1.000 28.174  ? 47  ILE   BBB CA  1 ? 
ATOM   2397 C  C   . ILE   B 1 48  ? 31.140  46.208 73.025 1.000 25.040  ? 47  ILE   BBB C   1 ? 
ATOM   2398 O  O   . ILE   B 1 48  ? 30.253  46.708 73.718 1.000 29.801  ? 47  ILE   BBB O   1 ? 
ATOM   2399 C  CB  . ILE   B 1 48  ? 30.462  43.757 72.442 1.000 36.775  ? 47  ILE   BBB CB  1 ? 
ATOM   2400 C  CG1 . ILE   B 1 48  ? 31.168  42.469 72.010 1.000 45.133  ? 47  ILE   BBB CG1 1 ? 
ATOM   2401 C  CG2 . ILE   B 1 48  ? 29.799  44.384 71.244 1.000 46.257  ? 47  ILE   BBB CG2 1 ? 
ATOM   2402 C  CD1 . ILE   B 1 48  ? 31.806  41.751 73.114 1.000 59.528  ? 47  ILE   BBB CD1 1 ? 
ATOM   2403 N  N   . SER   B 1 49  ? 31.893  46.891 72.170 1.000 27.633  ? 48  SER   BBB N   1 ? 
ATOM   2404 C  CA  . SER   B 1 49  ? 31.707  48.318 71.799 1.000 33.174  ? 48  SER   BBB CA  1 ? 
ATOM   2405 C  C   . SER   B 1 49  ? 31.405  48.307 70.293 1.000 30.236  ? 48  SER   BBB C   1 ? 
ATOM   2406 O  O   . SER   B 1 49  ? 32.247  47.791 69.520 1.000 31.428  ? 48  SER   BBB O   1 ? 
ATOM   2407 C  CB  . SER   B 1 49  ? 32.926  49.127 72.188 1.000 43.062  ? 48  SER   BBB CB  1 ? 
ATOM   2408 O  OG  . SER   B 1 49  ? 32.968  50.342 71.463 1.000 48.891  ? 48  SER   BBB OG  1 ? 
ATOM   2409 N  N   . VAL   B 1 50  ? 30.167  48.614 69.931 1.000 28.347  ? 49  VAL   BBB N   1 ? 
ATOM   2410 C  CA  . VAL   B 1 50  ? 29.843  48.893 68.502 1.000 28.668  ? 49  VAL   BBB CA  1 ? 
ATOM   2411 C  C   . VAL   B 1 50  ? 29.588  50.400 68.354 1.000 34.001  ? 49  VAL   BBB C   1 ? 
ATOM   2412 O  O   . VAL   B 1 50  ? 28.691  50.934 69.032 1.000 39.349  ? 49  VAL   BBB O   1 ? 
ATOM   2413 C  CB  . VAL   B 1 50  ? 28.655  48.084 67.968 1.000 29.755  ? 49  VAL   BBB CB  1 ? 
ATOM   2414 C  CG1 . VAL   B 1 50  ? 29.079  46.641 67.869 1.000 31.906  ? 49  VAL   BBB CG1 1 ? 
ATOM   2415 C  CG2 . VAL   B 1 50  ? 27.408  48.182 68.834 1.000 32.900  ? 49  VAL   BBB CG2 1 ? 
ATOM   2416 N  N   . SER   B 1 51  ? 30.431  51.015 67.511 1.000 36.491  ? 50  SER   BBB N   1 ? 
ATOM   2417 C  CA  A SER   B 1 51  ? 30.143  52.442 67.054 0.500 45.630  ? 50  SER   BBB CA  1 ? 
ATOM   2418 C  CA  B SER   B 1 51  ? 30.237  52.467 67.067 0.500 47.057  ? 50  SER   BBB CA  1 ? 
ATOM   2419 C  C   . SER   B 1 51  ? 30.248  52.478 65.442 1.000 50.483  ? 50  SER   BBB C   1 ? 
ATOM   2420 O  O   . SER   B 1 51  ? 31.364  52.096 64.772 1.000 47.442  ? 50  SER   BBB O   1 ? 
ATOM   2421 C  CB  A SER   B 1 51  ? 30.991  53.546 67.662 0.500 42.207  ? 50  SER   BBB CB  1 ? 
ATOM   2422 C  CB  B SER   B 1 51  ? 31.331  53.403 67.585 0.500 49.074  ? 50  SER   BBB CB  1 ? 
ATOM   2423 O  OG  A SER   B 1 51  ? 30.158  54.702 67.735 0.500 33.805  ? 50  SER   BBB OG  1 ? 
ATOM   2424 O  OG  B SER   B 1 51  ? 32.623  52.806 67.432 0.500 43.329  ? 50  SER   BBB OG  1 ? 
ATOM   2425 N  N   A TYR   B 1 52  ? 28.945  52.477 64.940 0.500 39.034  ? 51  TYR   BBB N   1 ? 
ATOM   2426 N  N   B TYR   B 1 52  ? 29.007  52.296 64.905 0.500 36.927  ? 51  TYR   BBB N   1 ? 
ATOM   2427 C  CA  A TYR   B 1 52  ? 28.611  52.328 63.501 0.500 36.008  ? 51  TYR   BBB CA  1 ? 
ATOM   2428 C  CA  B TYR   B 1 52  ? 28.954  52.297 63.436 0.500 31.847  ? 51  TYR   BBB CA  1 ? 
ATOM   2429 C  C   A TYR   B 1 52  ? 28.184  53.672 62.922 0.500 33.173  ? 51  TYR   BBB C   1 ? 
ATOM   2430 C  C   B TYR   B 1 52  ? 28.674  53.749 63.121 0.500 25.500  ? 51  TYR   BBB C   1 ? 
ATOM   2431 O  O   A TYR   B 1 52  ? 27.174  54.311 63.401 0.500 30.845  ? 51  TYR   BBB O   1 ? 
ATOM   2432 O  O   B TYR   B 1 52  ? 28.412  54.541 64.061 0.500 27.700  ? 51  TYR   BBB O   1 ? 
ATOM   2433 C  CB  A TYR   B 1 52  ? 27.449  51.369 63.253 0.500 29.759  ? 51  TYR   BBB CB  1 ? 
ATOM   2434 C  CB  B TYR   B 1 52  ? 27.982  51.286 62.847 0.500 29.441  ? 51  TYR   BBB CB  1 ? 
ATOM   2435 C  CG  A TYR   B 1 52  ? 27.672  49.947 63.673 0.500 26.158  ? 51  TYR   BBB CG  1 ? 
ATOM   2436 C  CG  B TYR   B 1 52  ? 28.260  49.878 63.298 0.500 21.634  ? 51  TYR   BBB CG  1 ? 
ATOM   2437 C  CD1 A TYR   B 1 52  ? 28.933  49.384 63.791 0.500 23.874  ? 51  TYR   BBB CD1 1 ? 
ATOM   2438 C  CD1 B TYR   B 1 52  ? 29.545  49.342 63.422 0.500 18.971  ? 51  TYR   BBB CD1 1 ? 
ATOM   2439 C  CD2 A TYR   B 1 52  ? 26.564  49.197 63.976 0.500 27.818  ? 51  TYR   BBB CD2 1 ? 
ATOM   2440 C  CD2 B TYR   B 1 52  ? 27.189  49.096 63.653 0.500 23.559  ? 51  TYR   BBB CD2 1 ? 
ATOM   2441 C  CE1 A TYR   B 1 52  ? 29.078  48.056 64.172 0.500 24.225  ? 51  TYR   BBB CE1 1 ? 
ATOM   2442 C  CE1 B TYR   B 1 52  ? 29.743  48.028 63.852 0.500 19.123  ? 51  TYR   BBB CE1 1 ? 
ATOM   2443 C  CE2 A TYR   B 1 52  ? 26.686  47.863 64.339 0.500 24.885  ? 51  TYR   BBB CE2 1 ? 
ATOM   2444 C  CE2 B TYR   B 1 52  ? 27.364  47.784 64.063 0.500 23.498  ? 51  TYR   BBB CE2 1 ? 
ATOM   2445 C  CZ  A TYR   B 1 52  ? 27.949  47.324 64.475 0.500 23.890  ? 51  TYR   BBB CZ  1 ? 
ATOM   2446 C  CZ  B TYR   B 1 52  ? 28.640  47.261 64.182 0.500 21.207  ? 51  TYR   BBB CZ  1 ? 
ATOM   2447 O  OH  A TYR   B 1 52  ? 28.081  46.009 64.825 0.500 23.493  ? 51  TYR   BBB OH  1 ? 
ATOM   2448 O  OH  B TYR   B 1 52  ? 28.750  45.951 64.589 0.500 22.893  ? 51  TYR   BBB OH  1 ? 
ATOM   2449 N  N   . ASN   B 1 53  ? 28.897  54.037 61.860 1.000 29.576  ? 52  ASN   BBB N   1 ? 
ATOM   2450 C  CA  . ASN   B 1 53  ? 28.689  55.330 61.205 1.000 33.081  ? 52  ASN   BBB CA  1 ? 
ATOM   2451 C  C   . ASN   B 1 53  ? 27.555  55.084 60.194 1.000 34.216  ? 52  ASN   BBB C   1 ? 
ATOM   2452 O  O   . ASN   B 1 53  ? 27.821  54.410 59.132 1.000 33.847  ? 52  ASN   BBB O   1 ? 
ATOM   2453 C  CB  . ASN   B 1 53  ? 30.039  55.779 60.623 1.000 33.205  ? 52  ASN   BBB CB  1 ? 
ATOM   2454 C  CG  . ASN   B 1 53  ? 29.970  57.213 60.147 1.000 29.174  ? 52  ASN   BBB CG  1 ? 
ATOM   2455 O  OD1 . ASN   B 1 53  ? 28.934  57.617 59.613 1.000 27.481  ? 52  ASN   BBB OD1 1 ? 
ATOM   2456 N  ND2 . ASN   B 1 53  ? 31.039  57.991 60.377 1.000 48.409  ? 52  ASN   BBB ND2 1 ? 
ATOM   2457 N  N   . PRO   B 1 54  ? 26.321  55.651 60.376 1.000 31.282  ? 53  PRO   BBB N   1 ? 
ATOM   2458 C  CA  . PRO   B 1 54  ? 25.226  55.313 59.465 1.000 35.781  ? 53  PRO   BBB CA  1 ? 
ATOM   2459 C  C   . PRO   B 1 54  ? 25.431  55.728 58.001 1.000 36.654  ? 53  PRO   BBB C   1 ? 
ATOM   2460 O  O   . PRO   B 1 54  ? 24.775  55.159 57.114 1.000 32.602  ? 53  PRO   BBB O   1 ? 
ATOM   2461 C  CB  . PRO   B 1 54  ? 24.009  56.011 60.082 1.000 41.746  ? 53  PRO   BBB CB  1 ? 
ATOM   2462 C  CG  . PRO   B 1 54  ? 24.654  57.253 60.741 1.000 35.343  ? 53  PRO   BBB CG  1 ? 
ATOM   2463 C  CD  . PRO   B 1 54  ? 25.925  56.691 61.367 1.000 36.260  ? 53  PRO   BBB CD  1 ? 
ATOM   2464 N  N   . ALA   B 1 55  ? 26.363  56.657 57.747 1.000 37.049  ? 54  ALA   BBB N   1 ? 
ATOM   2465 C  CA  . ALA   B 1 55  ? 26.770  57.002 56.369 1.000 33.186  ? 54  ALA   BBB CA  1 ? 
ATOM   2466 C  C   . ALA   B 1 55  ? 27.596  55.876 55.725 1.000 27.594  ? 54  ALA   BBB C   1 ? 
ATOM   2467 O  O   . ALA   B 1 55  ? 27.890  56.007 54.536 1.000 27.794  ? 54  ALA   BBB O   1 ? 
ATOM   2468 C  CB  . ALA   B 1 55  ? 27.528  58.319 56.376 1.000 31.911  ? 54  ALA   BBB CB  1 ? 
ATOM   2469 N  N   . THR   B 1 56  ? 27.971  54.808 56.445 1.000 27.741  ? 55  THR   BBB N   1 ? 
ATOM   2470 C  CA  . THR   B 1 56  ? 28.689  53.685 55.766 1.000 27.884  ? 55  THR   BBB CA  1 ? 
ATOM   2471 C  C   . THR   B 1 56  ? 27.679  52.738 55.102 1.000 24.599  ? 55  THR   BBB C   1 ? 
ATOM   2472 O  O   . THR   B 1 56  ? 28.143  52.030 54.230 1.000 24.364  ? 55  THR   BBB O   1 ? 
ATOM   2473 C  CB  . THR   B 1 56  ? 29.647  52.931 56.701 1.000 27.911  ? 55  THR   BBB CB  1 ? 
ATOM   2474 O  OG1 . THR   B 1 56  ? 28.816  52.468 57.831 1.000 30.090  ? 55  THR   BBB OG1 1 ? 
ATOM   2475 C  CG2 . THR   B 1 56  ? 30.836  53.785 57.155 1.000 27.572  ? 55  THR   BBB CG2 1 ? 
ATOM   2476 N  N   . ALA   B 1 57  ? 26.377  52.859 55.378 1.000 22.830  ? 56  ALA   BBB N   1 ? 
ATOM   2477 C  CA  . ALA   B 1 57  ? 25.376  51.968 54.712 1.000 23.500  ? 56  ALA   BBB CA  1 ? 
ATOM   2478 C  C   . ALA   B 1 57  ? 25.466  52.224 53.190 1.000 24.776  ? 56  ALA   BBB C   1 ? 
ATOM   2479 O  O   . ALA   B 1 57  ? 25.511  53.425 52.783 1.000 24.976  ? 56  ALA   BBB O   1 ? 
ATOM   2480 C  CB  . ALA   B 1 57  ? 24.001  52.244 55.239 1.000 26.406  ? 56  ALA   BBB CB  1 ? 
ATOM   2481 N  N   . LYS   B 1 58  ? 25.474  51.193 52.331 1.000 23.504  ? 57  LYS   BBB N   1 ? 
ATOM   2482 C  CA  . LYS   B 1 58  ? 25.702  51.380 50.878 1.000 23.003  ? 57  LYS   BBB CA  1 ? 
ATOM   2483 C  C   . LYS   B 1 58  ? 24.573  50.783 50.034 1.000 20.019  ? 57  LYS   BBB C   1 ? 
ATOM   2484 O  O   . LYS   B 1 58  ? 23.984  51.499 49.210 1.000 22.672  ? 57  LYS   BBB O   1 ? 
ATOM   2485 C  CB  . LYS   B 1 58  ? 27.074  50.803 50.532 1.000 27.032  ? 57  LYS   BBB CB  1 ? 
ATOM   2486 C  CG  . LYS   B 1 58  ? 27.525  50.931 49.080 1.000 29.854  ? 57  LYS   BBB CG  1 ? 
ATOM   2487 C  CD  . LYS   B 1 58  ? 28.956  50.416 48.910 1.000 42.363  ? 57  LYS   BBB CD  1 ? 
ATOM   2488 C  CE  . LYS   B 1 58  ? 29.439  50.429 47.476 1.000 54.143  ? 57  LYS   BBB CE  1 ? 
ATOM   2489 N  NZ  . LYS   B 1 58  ? 29.028  49.192 46.752 1.000 63.236  ? 57  LYS   BBB NZ  1 ? 
ATOM   2490 N  N   . GLU   B 1 59  ? 24.346  49.439 50.135 1.000 19.423  ? 58  GLU   BBB N   1 ? 
ATOM   2491 C  CA  . GLU   B 1 59  ? 23.535  48.761 49.107 1.000 19.623  ? 58  GLU   BBB CA  1 ? 
ATOM   2492 C  C   . GLU   B 1 59  ? 22.847  47.546 49.737 1.000 18.159  ? 58  GLU   BBB C   1 ? 
ATOM   2493 O  O   . GLU   B 1 59  ? 23.395  46.973 50.688 1.000 20.080  ? 58  GLU   BBB O   1 ? 
ATOM   2494 C  CB  . GLU   B 1 59  ? 24.477  48.316 47.994 1.000 21.962  ? 58  GLU   BBB CB  1 ? 
ATOM   2495 C  CG  . GLU   B 1 59  ? 23.811  47.607 46.828 1.000 24.240  ? 58  GLU   BBB CG  1 ? 
ATOM   2496 C  CD  . GLU   B 1 59  ? 24.737  47.518 45.629 1.000 27.458  ? 58  GLU   BBB CD  1 ? 
ATOM   2497 O  OE1 . GLU   B 1 59  ? 25.489  46.518 45.533 1.000 31.163  ? 58  GLU   BBB OE1 1 ? 
ATOM   2498 O  OE2 . GLU   B 1 59  ? 24.757  48.486 44.816 1.000 36.909  ? 58  GLU   BBB OE2 1 ? 
ATOM   2499 N  N   . ILE   B 1 60  ? 21.661  47.256 49.250 1.000 18.340  ? 59  ILE   BBB N   1 ? 
ATOM   2500 C  CA  . ILE   B 1 60  ? 20.934  46.010 49.595 1.000 17.343  ? 59  ILE   BBB CA  1 ? 
ATOM   2501 C  C   . ILE   B 1 60  ? 20.844  45.179 48.319 1.000 20.754  ? 59  ILE   BBB C   1 ? 
ATOM   2502 O  O   . ILE   B 1 60  ? 20.627  45.742 47.220 1.000 19.799  ? 59  ILE   BBB O   1 ? 
ATOM   2503 C  CB  . ILE   B 1 60  ? 19.571  46.299 50.250 1.000 18.279  ? 59  ILE   BBB CB  1 ? 
ATOM   2504 C  CG1 . ILE   B 1 60  ? 18.970  45.042 50.874 1.000 21.142  ? 59  ILE   BBB CG1 1 ? 
ATOM   2505 C  CG2 . ILE   B 1 60  ? 18.578  46.922 49.282 1.000 19.368  ? 59  ILE   BBB CG2 1 ? 
ATOM   2506 C  CD1 . ILE   B 1 60  ? 17.741  45.280 51.709 1.000 22.086  ? 59  ILE   BBB CD1 1 ? 
ATOM   2507 N  N   . ILE   B 1 61  ? 21.103  43.867 48.454 1.000 21.338  ? 60  ILE   BBB N   1 ? 
ATOM   2508 C  CA  . ILE   B 1 61  ? 21.206  42.991 47.260 1.000 17.560  ? 60  ILE   BBB CA  1 ? 
ATOM   2509 C  C   . ILE   B 1 61  ? 20.638  41.596 47.562 1.000 16.399  ? 60  ILE   BBB C   1 ? 
ATOM   2510 O  O   . ILE   B 1 61  ? 20.815  41.126 48.692 1.000 18.804  ? 60  ILE   BBB O   1 ? 
ATOM   2511 C  CB  . ILE   B 1 61  ? 22.666  42.926 46.788 1.000 19.042  ? 60  ILE   BBB CB  1 ? 
ATOM   2512 C  CG1 . ILE   B 1 61  ? 22.814  42.072 45.535 1.000 20.445  ? 60  ILE   BBB CG1 1 ? 
ATOM   2513 C  CG2 . ILE   B 1 61  ? 23.591  42.492 47.896 1.000 21.490  ? 60  ILE   BBB CG2 1 ? 
ATOM   2514 C  CD1 . ILE   B 1 61  ? 24.079  42.282 44.822 1.000 24.466  ? 60  ILE   BBB CD1 1 ? 
ATOM   2515 N  N   . ASN   B 1 62  ? 19.913  41.088 46.574 1.000 17.271  ? 61  ASN   BBB N   1 ? 
ATOM   2516 C  CA  . ASN   B 1 62  ? 19.348  39.717 46.603 1.000 17.032  ? 61  ASN   BBB CA  1 ? 
ATOM   2517 C  C   . ASN   B 1 62  ? 20.450  38.821 46.043 1.000 17.147  ? 61  ASN   BBB C   1 ? 
ATOM   2518 O  O   . ASN   B 1 62  ? 20.825  39.005 44.861 1.000 19.541  ? 61  ASN   BBB O   1 ? 
ATOM   2519 C  CB  . ASN   B 1 62  ? 18.058  39.702 45.800 1.000 19.525  ? 61  ASN   BBB CB  1 ? 
ATOM   2520 C  CG  . ASN   B 1 62  ? 17.397  38.361 45.696 1.000 18.200  ? 61  ASN   BBB CG  1 ? 
ATOM   2521 O  OD1 . ASN   B 1 62  ? 18.113  37.349 45.706 1.000 18.986  ? 61  ASN   BBB OD1 1 ? 
ATOM   2522 N  ND2 . ASN   B 1 62  ? 16.078  38.375 45.608 1.000 18.727  ? 61  ASN   BBB ND2 1 ? 
ATOM   2523 N  N   . VAL   B 1 63  ? 20.963  37.921 46.882 1.000 18.725  ? 62  VAL   BBB N   1 ? 
ATOM   2524 C  CA  . VAL   B 1 63  ? 22.075  37.001 46.507 1.000 20.279  ? 62  VAL   BBB CA  1 ? 
ATOM   2525 C  C   . VAL   B 1 63  ? 21.542  35.584 46.218 1.000 18.993  ? 62  VAL   BBB C   1 ? 
ATOM   2526 O  O   . VAL   B 1 63  ? 22.354  34.653 46.085 1.000 22.828  ? 62  VAL   BBB O   1 ? 
ATOM   2527 C  CB  . VAL   B 1 63  ? 23.180  37.068 47.575 1.000 19.214  ? 62  VAL   BBB CB  1 ? 
ATOM   2528 C  CG1 . VAL   B 1 63  ? 23.746  38.495 47.618 1.000 21.919  ? 62  VAL   BBB CG1 1 ? 
ATOM   2529 C  CG2 . VAL   B 1 63  ? 22.700  36.654 48.955 1.000 20.721  ? 62  VAL   BBB CG2 1 ? 
ATOM   2530 N  N   . GLY   B 1 64  ? 20.256  35.454 45.990 1.000 18.263  ? 63  GLY   BBB N   1 ? 
ATOM   2531 C  CA  . GLY   B 1 64  ? 19.633  34.186 45.576 1.000 22.162  ? 63  GLY   BBB CA  1 ? 
ATOM   2532 C  C   . GLY   B 1 64  ? 19.243  33.313 46.755 1.000 19.395  ? 63  GLY   BBB C   1 ? 
ATOM   2533 O  O   . GLY   B 1 64  ? 18.074  32.864 46.767 1.000 23.484  ? 63  GLY   BBB O   1 ? 
ATOM   2534 N  N   . HIS   B 1 65  ? 20.145  33.059 47.689 1.000 18.735  ? 64  HIS   BBB N   1 ? 
ATOM   2535 C  CA  . HIS   B 1 65  ? 19.831  32.287 48.918 1.000 20.286  ? 64  HIS   BBB CA  1 ? 
ATOM   2536 C  C   . HIS   B 1 65  ? 19.450  33.180 50.091 1.000 19.706  ? 64  HIS   BBB C   1 ? 
ATOM   2537 O  O   . HIS   B 1 65  ? 18.976  32.684 51.116 1.000 23.596  ? 64  HIS   BBB O   1 ? 
ATOM   2538 C  CB  . HIS   B 1 65  ? 21.050  31.456 49.290 1.000 20.840  ? 64  HIS   BBB CB  1 ? 
ATOM   2539 C  CG  . HIS   B 1 65  ? 22.247  32.266 49.660 1.000 18.731  ? 64  HIS   BBB CG  1 ? 
ATOM   2540 N  ND1 . HIS   B 1 65  ? 23.213  32.656 48.739 1.000 24.672  ? 64  HIS   BBB ND1 1 ? 
ATOM   2541 C  CD2 . HIS   B 1 65  ? 22.666  32.662 50.872 1.000 18.727  ? 64  HIS   BBB CD2 1 ? 
ATOM   2542 C  CE1 . HIS   B 1 65  ? 24.184  33.297 49.377 1.000 21.298  ? 64  HIS   BBB CE1 1 ? 
ATOM   2543 N  NE2 . HIS   B 1 65  ? 23.858  33.335 50.688 1.000 23.929  ? 64  HIS   BBB NE2 1 ? 
ATOM   2544 N  N   . SER   B 1 66  ? 19.714  34.494 49.965 1.000 18.398  ? 65  SER   BBB N   1 ? 
ATOM   2545 C  CA  . SER   B 1 66  ? 19.513  35.465 51.067 1.000 18.898  ? 65  SER   BBB CA  1 ? 
ATOM   2546 C  C   . SER   B 1 66  ? 19.463  36.859 50.452 1.000 17.649  ? 65  SER   BBB C   1 ? 
ATOM   2547 O  O   . SER   B 1 66  ? 19.451  36.990 49.201 1.000 18.255  ? 65  SER   BBB O   1 ? 
ATOM   2548 C  CB  . SER   B 1 66  ? 20.610  35.357 52.101 1.000 20.488  ? 65  SER   BBB CB  1 ? 
ATOM   2549 O  OG  . SER   B 1 66  ? 20.253  35.961 53.331 1.000 20.656  ? 65  SER   BBB OG  1 ? 
ATOM   2550 N  N   . PHE   B 1 67  ? 19.450  37.858 51.325 1.000 17.132  ? 66  PHE   BBB N   1 ? 
ATOM   2551 C  CA  . PHE   B 1 67  ? 19.709  39.257 50.906 1.000 17.698  ? 66  PHE   BBB CA  1 ? 
ATOM   2552 C  C   . PHE   B 1 67  ? 20.726  39.793 51.893 1.000 16.997  ? 66  PHE   BBB C   1 ? 
ATOM   2553 O  O   . PHE   B 1 67  ? 20.702  39.401 53.082 1.000 18.745  ? 66  PHE   BBB O   1 ? 
ATOM   2554 C  CB  . PHE   B 1 67  ? 18.426  40.094 50.830 1.000 16.973  ? 66  PHE   BBB CB  1 ? 
ATOM   2555 C  CG  . PHE   B 1 67  ? 17.831  40.435 52.162 1.000 17.284  ? 66  PHE   BBB CG  1 ? 
ATOM   2556 C  CD1 . PHE   B 1 67  ? 16.940  39.593 52.799 1.000 19.002  ? 66  PHE   BBB CD1 1 ? 
ATOM   2557 C  CD2 . PHE   B 1 67  ? 18.199  41.612 52.790 1.000 18.251  ? 66  PHE   BBB CD2 1 ? 
ATOM   2558 C  CE1 . PHE   B 1 67  ? 16.453  39.899 54.054 1.000 18.425  ? 66  PHE   BBB CE1 1 ? 
ATOM   2559 C  CE2 . PHE   B 1 67  ? 17.681  41.949 54.025 1.000 20.019  ? 66  PHE   BBB CE2 1 ? 
ATOM   2560 C  CZ  . PHE   B 1 67  ? 16.760  41.128 54.636 1.000 21.298  ? 66  PHE   BBB CZ  1 ? 
ATOM   2561 N  N   . HIS   B 1 68  ? 21.533  40.749 51.413 1.000 16.738  ? 67  HIS   BBB N   1 ? 
ATOM   2562 C  CA  . HIS   B 1 68  ? 22.615  41.324 52.212 1.000 17.679  ? 67  HIS   BBB CA  1 ? 
ATOM   2563 C  C   . HIS   B 1 68  ? 22.471  42.858 52.193 1.000 16.444  ? 67  HIS   BBB C   1 ? 
ATOM   2564 O  O   . HIS   B 1 68  ? 22.073  43.369 51.129 1.000 19.607  ? 67  HIS   BBB O   1 ? 
ATOM   2565 C  CB  . HIS   B 1 68  ? 23.966  40.944 51.621 1.000 17.429  ? 67  HIS   BBB CB  1 ? 
ATOM   2566 C  CG  . HIS   B 1 68  ? 24.308  39.498 51.713 1.000 18.279  ? 67  HIS   BBB CG  1 ? 
ATOM   2567 N  ND1 . HIS   B 1 68  ? 25.392  38.991 51.067 1.000 18.958  ? 67  HIS   BBB ND1 1 ? 
ATOM   2568 C  CD2 . HIS   B 1 68  ? 23.785  38.513 52.474 1.000 18.563  ? 67  HIS   BBB CD2 1 ? 
ATOM   2569 C  CE1 . HIS   B 1 68  ? 25.447  37.651 51.321 1.000 20.062  ? 67  HIS   BBB CE1 1 ? 
ATOM   2570 N  NE2 . HIS   B 1 68  ? 24.516  37.372 52.217 1.000 21.253  ? 67  HIS   BBB NE2 1 ? 
ATOM   2571 N  N   . VAL   B 1 69  ? 22.787  43.427 53.335 1.000 17.303  ? 68  VAL   BBB N   1 ? 
ATOM   2572 C  CA  . VAL   B 1 69  ? 22.973  44.922 53.369 1.000 18.867  ? 68  VAL   BBB CA  1 ? 
ATOM   2573 C  C   . VAL   B 1 69  ? 24.464  45.131 53.534 1.000 17.737  ? 68  VAL   BBB C   1 ? 
ATOM   2574 O  O   . VAL   B 1 69  ? 25.007  44.775 54.619 1.000 19.199  ? 68  VAL   BBB O   1 ? 
ATOM   2575 C  CB  . VAL   B 1 69  ? 22.153  45.499 54.515 1.000 19.295  ? 68  VAL   BBB CB  1 ? 
ATOM   2576 C  CG1 . VAL   B 1 69  ? 22.401  47.016 54.580 1.000 20.975  ? 68  VAL   BBB CG1 1 ? 
ATOM   2577 C  CG2 . VAL   B 1 69  ? 20.689  45.196 54.354 1.000 20.423  ? 68  VAL   BBB CG2 1 ? 
ATOM   2578 N  N   . ASN   B 1 70  ? 25.078  45.759 52.519 1.000 17.581  ? 69  ASN   BBB N   1 ? 
ATOM   2579 C  CA  . ASN   B 1 70  ? 26.535  45.912 52.449 1.000 19.440  ? 69  ASN   BBB CA  1 ? 
ATOM   2580 C  C   . ASN   B 1 70  ? 26.911  47.332 52.841 1.000 17.235  ? 69  ASN   BBB C   1 ? 
ATOM   2581 O  O   . ASN   B 1 70  ? 26.069  48.294 52.561 1.000 19.344  ? 69  ASN   BBB O   1 ? 
ATOM   2582 C  CB  . ASN   B 1 70  ? 27.054  45.517 51.065 1.000 20.051  ? 69  ASN   BBB CB  1 ? 
ATOM   2583 C  CG  . ASN   B 1 70  ? 26.976  44.016 50.942 1.000 18.008  ? 69  ASN   BBB CG  1 ? 
ATOM   2584 O  OD1 . ASN   B 1 70  ? 27.349  43.380 51.901 1.000 25.580  ? 69  ASN   BBB OD1 1 ? 
ATOM   2585 N  ND2 . ASN   B 1 70  ? 26.552  43.539 49.799 1.000 20.006  ? 69  ASN   BBB ND2 1 ? 
ATOM   2586 N  N   . PHE   B 1 71  ? 28.059  47.439 53.489 1.000 19.151  ? 70  PHE   BBB N   1 ? 
ATOM   2587 C  CA  . PHE   B 1 71  ? 28.581  48.755 53.972 1.000 24.422  ? 70  PHE   BBB CA  1 ? 
ATOM   2588 C  C   . PHE   B 1 71  ? 29.907  49.071 53.308 1.000 24.203  ? 70  PHE   BBB C   1 ? 
ATOM   2589 O  O   . PHE   B 1 71  ? 30.688  48.225 52.963 1.000 24.711  ? 70  PHE   BBB O   1 ? 
ATOM   2590 C  CB  . PHE   B 1 71  ? 28.762  48.771 55.492 1.000 25.218  ? 70  PHE   BBB CB  1 ? 
ATOM   2591 C  CG  . PHE   B 1 71  ? 27.452  48.633 56.224 1.000 24.088  ? 70  PHE   BBB CG  1 ? 
ATOM   2592 C  CD1 . PHE   B 1 71  ? 26.749  47.417 56.221 1.000 23.094  ? 70  PHE   BBB CD1 1 ? 
ATOM   2593 C  CD2 . PHE   B 1 71  ? 26.919  49.708 56.913 1.000 22.674  ? 70  PHE   BBB CD2 1 ? 
ATOM   2594 C  CE1 . PHE   B 1 71  ? 25.516  47.331 56.839 1.000 24.342  ? 70  PHE   BBB CE1 1 ? 
ATOM   2595 C  CE2 . PHE   B 1 71  ? 25.688  49.634 57.536 1.000 24.275  ? 70  PHE   BBB CE2 1 ? 
ATOM   2596 C  CZ  . PHE   B 1 71  ? 25.007  48.430 57.521 1.000 23.150  ? 70  PHE   BBB CZ  1 ? 
ATOM   2597 N  N   . GLU   B 1 72  ? 30.154  50.387 53.141 1.000 22.607  ? 71  GLU   BBB N   1 ? 
ATOM   2598 C  CA  . GLU   B 1 72  ? 31.460  50.882 52.659 1.000 27.073  ? 71  GLU   BBB CA  1 ? 
ATOM   2599 C  C   . GLU   B 1 72  ? 32.517  50.443 53.716 1.000 31.017  ? 71  GLU   BBB C   1 ? 
ATOM   2600 O  O   . GLU   B 1 72  ? 32.340  50.692 54.884 1.000 37.297  ? 71  GLU   BBB O   1 ? 
ATOM   2601 C  CB  . GLU   B 1 72  ? 31.428  52.415 52.543 1.000 28.901  ? 71  GLU   BBB CB  1 ? 
ATOM   2602 C  CG  . GLU   B 1 72  ? 30.426  52.939 51.510 1.000 38.334  ? 71  GLU   BBB CG  1 ? 
ATOM   2603 C  CD  . GLU   B 1 72  ? 30.263  54.463 51.365 1.000 50.821  ? 71  GLU   BBB CD  1 ? 
ATOM   2604 O  OE1 . GLU   B 1 72  ? 30.908  55.249 52.125 1.000 60.315  ? 71  GLU   BBB OE1 1 ? 
ATOM   2605 O  OE2 . GLU   B 1 72  ? 29.486  54.881 50.468 1.000 62.294  ? 71  GLU   BBB OE2 1 ? 
ATOM   2606 N  N   . ASP   B 1 73  ? 33.617  49.856 53.275 1.000 34.869  ? 72  ASP   BBB N   1 ? 
ATOM   2607 C  CA  . ASP   B 1 73  ? 34.625  49.214 54.216 1.000 40.791  ? 72  ASP   BBB CA  1 ? 
ATOM   2608 C  C   . ASP   B 1 73  ? 36.050  49.620 53.810 1.000 50.077  ? 72  ASP   BBB C   1 ? 
ATOM   2609 O  O   . ASP   B 1 73  ? 37.031  48.839 54.151 1.000 48.578  ? 72  ASP   BBB O   1 ? 
ATOM   2610 C  CB  . ASP   B 1 73  ? 34.480  47.673 54.291 1.000 37.629  ? 72  ASP   BBB CB  1 ? 
ATOM   2611 C  CG  . ASP   B 1 73  ? 34.869  46.985 52.993 1.000 40.136  ? 72  ASP   BBB CG  1 ? 
ATOM   2612 O  OD1 . ASP   B 1 73  ? 34.544  47.537 51.948 1.000 38.408  ? 72  ASP   BBB OD1 1 ? 
ATOM   2613 O  OD2 . ASP   B 1 73  ? 35.517  45.929 53.041 1.000 50.216  ? 72  ASP   BBB OD2 1 ? 
ATOM   2614 N  N   . ASN   B 1 74  ? 36.165  50.767 53.120 1.000 43.371  ? 73  ASN   BBB N   1 ? 
ATOM   2615 C  CA  . ASN   B 1 74  ? 37.482  51.287 52.672 1.000 47.135  ? 73  ASN   BBB CA  1 ? 
ATOM   2616 C  C   . ASN   B 1 74  ? 38.188  51.949 53.872 1.000 45.380  ? 73  ASN   BBB C   1 ? 
ATOM   2617 O  O   . ASN   B 1 74  ? 39.414  52.162 53.776 1.000 45.952  ? 73  ASN   BBB O   1 ? 
ATOM   2618 C  CB  . ASN   B 1 74  ? 37.369  52.184 51.432 1.000 57.251  ? 73  ASN   BBB CB  1 ? 
ATOM   2619 C  CG  . ASN   B 1 74  ? 36.712  53.519 51.707 1.000 75.659  ? 73  ASN   BBB CG  1 ? 
ATOM   2620 O  OD1 . ASN   B 1 74  ? 35.636  53.576 52.305 1.000 80.086  ? 73  ASN   BBB OD1 1 ? 
ATOM   2621 N  ND2 . ASN   B 1 74  ? 37.345  54.594 51.256 1.000 96.729  ? 73  ASN   BBB ND2 1 ? 
ATOM   2622 N  N   . ASP   B 1 75  ? 37.474  52.239 54.972 1.000 38.113  ? 74  ASP   BBB N   1 ? 
ATOM   2623 C  CA  . ASP   B 1 75  ? 38.099  52.781 56.207 1.000 36.444  ? 74  ASP   BBB CA  1 ? 
ATOM   2624 C  C   . ASP   B 1 75  ? 37.433  52.210 57.463 1.000 38.364  ? 74  ASP   BBB C   1 ? 
ATOM   2625 O  O   . ASP   B 1 75  ? 36.467  51.464 57.323 1.000 41.291  ? 74  ASP   BBB O   1 ? 
ATOM   2626 C  CB  . ASP   B 1 75  ? 38.058  54.319 56.223 1.000 42.838  ? 74  ASP   BBB CB  1 ? 
ATOM   2627 C  CG  . ASP   B 1 75  ? 36.674  54.955 56.172 1.000 43.715  ? 74  ASP   BBB CG  1 ? 
ATOM   2628 O  OD1 . ASP   B 1 75  ? 35.714  54.428 56.786 1.000 37.858  ? 74  ASP   BBB OD1 1 ? 
ATOM   2629 O  OD2 . ASP   B 1 75  ? 36.565  56.005 55.549 1.000 54.161  ? 74  ASP   BBB OD2 1 ? 
ATOM   2630 N  N   . ASN   B 1 76  ? 37.936  52.584 58.643 1.000 36.439  ? 75  ASN   BBB N   1 ? 
ATOM   2631 C  CA  . ASN   B 1 76  ? 37.434  52.076 59.949 1.000 30.220  ? 75  ASN   BBB CA  1 ? 
ATOM   2632 C  C   . ASN   B 1 76  ? 36.487  53.109 60.596 1.000 23.807  ? 75  ASN   BBB C   1 ? 
ATOM   2633 O  O   . ASN   B 1 76  ? 36.584  53.233 61.789 1.000 41.043  ? 75  ASN   BBB O   1 ? 
ATOM   2634 C  CB  . ASN   B 1 76  ? 38.546  51.779 60.964 1.000 33.575  ? 75  ASN   BBB CB  1 ? 
ATOM   2635 C  CG  . ASN   B 1 76  ? 39.593  50.813 60.454 1.000 46.582  ? 75  ASN   BBB CG  1 ? 
ATOM   2636 O  OD1 . ASN   B 1 76  ? 39.274  49.704 60.005 1.000 49.222  ? 75  ASN   BBB OD1 1 ? 
ATOM   2637 N  ND2 . ASN   B 1 76  ? 40.853  51.215 60.523 1.000 56.417  ? 75  ASN   BBB ND2 1 ? 
ATOM   2638 N  N   . ARG   B 1 77  ? 35.543  53.714 59.783 1.000 33.001  ? 76  ARG   BBB N   1 ? 
ATOM   2639 C  CA  . ARG   B 1 77  ? 34.421  54.573 60.335 1.000 34.743  ? 76  ARG   BBB CA  1 ? 
ATOM   2640 C  C   . ARG   B 1 77  ? 33.441  53.746 61.202 1.000 34.615  ? 76  ARG   BBB C   1 ? 
ATOM   2641 O  O   . ARG   B 1 77  ? 32.789  54.309 62.123 1.000 33.740  ? 76  ARG   BBB O   1 ? 
ATOM   2642 C  CB  . ARG   B 1 77  ? 33.593  55.227 59.215 1.000 39.791  ? 76  ARG   BBB CB  1 ? 
ATOM   2643 C  CG  . ARG   B 1 77  ? 34.053  56.646 58.840 1.000 43.314  ? 76  ARG   BBB CG  1 ? 
ATOM   2644 C  CD  . ARG   B 1 77  ? 33.263  57.229 57.676 1.000 42.993  ? 76  ARG   BBB CD  1 ? 
ATOM   2645 N  NE  . ARG   B 1 77  ? 33.398  56.409 56.498 1.000 35.806  ? 76  ARG   BBB NE  1 ? 
ATOM   2646 C  CZ  . ARG   B 1 77  ? 32.563  56.403 55.452 1.000 38.249  ? 76  ARG   BBB CZ  1 ? 
ATOM   2647 N  NH1 . ARG   B 1 77  ? 31.541  57.258 55.387 1.000 33.494  ? 76  ARG   BBB NH1 1 ? 
ATOM   2648 N  NH2 . ARG   B 1 77  ? 32.744  55.524 54.467 1.000 35.938  ? 76  ARG   BBB NH2 1 ? 
ATOM   2649 N  N   . SER   B 1 78  ? 33.234  52.479 60.835 1.000 31.234  ? 77  SER   BBB N   1 ? 
ATOM   2650 C  CA  . SER   B 1 78  ? 32.244  51.580 61.480 1.000 29.733  ? 77  SER   BBB CA  1 ? 
ATOM   2651 C  C   . SER   B 1 78  ? 32.976  50.348 62.002 1.000 26.079  ? 77  SER   BBB C   1 ? 
ATOM   2652 O  O   . SER   B 1 78  ? 33.456  49.619 61.159 1.000 25.403  ? 77  SER   BBB O   1 ? 
ATOM   2653 C  CB  . SER   B 1 78  ? 31.208  51.166 60.485 1.000 26.701  ? 77  SER   BBB CB  1 ? 
ATOM   2654 O  OG  . SER   B 1 78  ? 30.296  52.290 60.178 1.000 29.243  ? 77  SER   BBB OG  1 ? 
ATOM   2655 N  N   . VAL   B 1 79  ? 33.135  50.221 63.317 1.000 29.588  ? 78  VAL   BBB N   1 ? 
ATOM   2656 C  CA  . VAL   B 1 79  ? 34.003  49.193 63.936 1.000 30.673  ? 78  VAL   BBB CA  1 ? 
ATOM   2657 C  C   . VAL   B 1 79  ? 33.293  48.571 65.131 1.000 29.865  ? 78  VAL   BBB C   1 ? 
ATOM   2658 O  O   . VAL   B 1 79  ? 32.454  49.226 65.821 1.000 28.073  ? 78  VAL   BBB O   1 ? 
ATOM   2659 C  CB  . VAL   B 1 79  ? 35.404  49.676 64.350 1.000 35.194  ? 78  VAL   BBB CB  1 ? 
ATOM   2660 C  CG1 . VAL   B 1 79  ? 36.264  49.972 63.136 1.000 41.278  ? 78  VAL   BBB CG1 1 ? 
ATOM   2661 C  CG2 . VAL   B 1 79  ? 35.331  50.835 65.316 1.000 46.262  ? 78  VAL   BBB CG2 1 ? 
ATOM   2662 N  N   . LEU   B 1 80  ? 33.692  47.313 65.303 1.000 28.163  ? 79  LEU   BBB N   1 ? 
ATOM   2663 C  CA  . LEU   B 1 80  ? 33.429  46.480 66.494 1.000 25.770  ? 79  LEU   BBB CA  1 ? 
ATOM   2664 C  C   . LEU   B 1 80  ? 34.783  46.356 67.257 1.000 24.787  ? 79  LEU   BBB C   1 ? 
ATOM   2665 O  O   . LEU   B 1 80  ? 35.801  46.102 66.619 1.000 27.815  ? 79  LEU   BBB O   1 ? 
ATOM   2666 C  CB  . LEU   B 1 80  ? 32.929  45.109 66.034 1.000 25.755  ? 79  LEU   BBB CB  1 ? 
ATOM   2667 C  CG  . LEU   B 1 80  ? 32.968  44.003 67.081 1.000 24.804  ? 79  LEU   BBB CG  1 ? 
ATOM   2668 C  CD1 . LEU   B 1 80  ? 32.065  44.338 68.254 1.000 25.065  ? 79  LEU   BBB CD1 1 ? 
ATOM   2669 C  CD2 . LEU   B 1 80  ? 32.593  42.636 66.483 1.000 26.263  ? 79  LEU   BBB CD2 1 ? 
ATOM   2670 N  N   . LYS   B 1 81  ? 34.719  46.477 68.568 1.000 27.353  ? 80  LYS   BBB N   1 ? 
ATOM   2671 C  CA  . LYS   B 1 81  ? 35.934  46.319 69.424 1.000 28.914  ? 80  LYS   BBB CA  1 ? 
ATOM   2672 C  C   . LYS   B 1 81  ? 35.457  45.761 70.777 1.000 23.092  ? 80  LYS   BBB C   1 ? 
ATOM   2673 O  O   . LYS   B 1 81  ? 34.222  45.676 71.001 1.000 26.252  ? 80  LYS   BBB O   1 ? 
ATOM   2674 C  CB  . LYS   B 1 81  ? 36.790  47.594 69.537 1.000 39.252  ? 80  LYS   BBB CB  1 ? 
ATOM   2675 C  CG  . LYS   B 1 81  ? 36.017  48.883 69.678 1.000 48.213  ? 80  LYS   BBB CG  1 ? 
ATOM   2676 C  CD  . LYS   B 1 81  ? 36.944  50.098 69.775 1.000 52.680  ? 80  LYS   BBB CD  1 ? 
ATOM   2677 C  CE  . LYS   B 1 81  ? 36.212  51.419 69.879 1.000 67.815  ? 80  LYS   BBB CE  1 ? 
ATOM   2678 N  NZ  . LYS   B 1 81  ? 37.124  52.530 70.251 1.000 68.508  ? 80  LYS   BBB NZ  1 ? 
ATOM   2679 N  N   . GLY   B 1 82  ? 36.423  45.400 71.603 1.000 27.402  ? 81  GLY   BBB N   1 ? 
ATOM   2680 C  CA  . GLY   B 1 82  ? 36.173  44.841 72.943 1.000 25.876  ? 81  GLY   BBB CA  1 ? 
ATOM   2681 C  C   . GLY   B 1 82  ? 35.855  43.367 72.857 1.000 23.308  ? 81  GLY   BBB C   1 ? 
ATOM   2682 O  O   . GLY   B 1 82  ? 36.332  42.758 71.896 1.000 23.350  ? 81  GLY   BBB O   1 ? 
ATOM   2683 N  N   . GLY   B 1 83  ? 35.068  42.856 73.793 1.000 22.300  ? 82  GLY   BBB N   1 ? 
ATOM   2684 C  CA  . GLY   B 1 83  ? 34.820  41.400 73.895 1.000 22.429  ? 82  GLY   BBB CA  1 ? 
ATOM   2685 C  C   . GLY   B 1 83  ? 36.156  40.681 73.947 1.000 24.913  ? 82  GLY   BBB C   1 ? 
ATOM   2686 O  O   . GLY   B 1 83  ? 37.037  41.063 74.726 1.000 25.518  ? 82  GLY   BBB O   1 ? 
ATOM   2687 N  N   . PRO   B 1 84  ? 36.341  39.659 73.084 1.000 25.025  ? 83  PRO   BBB N   1 ? 
ATOM   2688 C  CA  . PRO   B 1 84  ? 37.561  38.852 73.089 1.000 27.056  ? 83  PRO   BBB CA  1 ? 
ATOM   2689 C  C   . PRO   B 1 84  ? 38.720  39.466 72.294 1.000 28.329  ? 83  PRO   BBB C   1 ? 
ATOM   2690 O  O   . PRO   B 1 84  ? 39.777  38.883 72.276 1.000 31.686  ? 83  PRO   BBB O   1 ? 
ATOM   2691 C  CB  . PRO   B 1 84  ? 37.091  37.563 72.394 1.000 27.457  ? 83  PRO   BBB CB  1 ? 
ATOM   2692 C  CG  . PRO   B 1 84  ? 36.052  38.036 71.398 1.000 25.574  ? 83  PRO   BBB CG  1 ? 
ATOM   2693 C  CD  . PRO   B 1 84  ? 35.381  39.234 72.058 1.000 25.712  ? 83  PRO   BBB CD  1 ? 
ATOM   2694 N  N   . PHE   B 1 85  ? 38.470  40.581 71.603 1.000 25.645  ? 84  PHE   BBB N   1 ? 
ATOM   2695 C  CA  . PHE   B 1 85  ? 39.376  41.196 70.589 1.000 27.471  ? 84  PHE   BBB CA  1 ? 
ATOM   2696 C  C   . PHE   B 1 85  ? 40.321  42.226 71.213 1.000 31.794  ? 84  PHE   BBB C   1 ? 
ATOM   2697 O  O   . PHE   B 1 85  ? 39.895  43.032 72.025 1.000 34.014  ? 84  PHE   BBB O   1 ? 
ATOM   2698 C  CB  . PHE   B 1 85  ? 38.559  41.926 69.517 1.000 27.862  ? 84  PHE   BBB CB  1 ? 
ATOM   2699 C  CG  . PHE   B 1 85  ? 37.488  41.066 68.896 1.000 26.516  ? 84  PHE   BBB CG  1 ? 
ATOM   2700 C  CD1 . PHE   B 1 85  ? 37.840  39.875 68.270 1.000 31.970  ? 84  PHE   BBB CD1 1 ? 
ATOM   2701 C  CD2 . PHE   B 1 85  ? 36.145  41.379 69.015 1.000 30.339  ? 84  PHE   BBB CD2 1 ? 
ATOM   2702 C  CE1 . PHE   B 1 85  ? 36.882  39.059 67.698 1.000 30.065  ? 84  PHE   BBB CE1 1 ? 
ATOM   2703 C  CE2 . PHE   B 1 85  ? 35.180  40.537 68.470 1.000 29.370  ? 84  PHE   BBB CE2 1 ? 
ATOM   2704 C  CZ  . PHE   B 1 85  ? 35.550  39.391 67.806 1.000 31.492  ? 84  PHE   BBB CZ  1 ? 
ATOM   2705 N  N   . SER   B 1 86  ? 41.570  42.245 70.781 1.000 36.032  ? 85  SER   BBB N   1 ? 
ATOM   2706 C  CA  . SER   B 1 86  ? 42.479  43.387 71.045 1.000 36.456  ? 85  SER   BBB CA  1 ? 
ATOM   2707 C  C   . SER   B 1 86  ? 42.472  44.341 69.843 1.000 39.920  ? 85  SER   BBB C   1 ? 
ATOM   2708 O  O   . SER   B 1 86  ? 42.795  45.503 70.044 1.000 48.765  ? 85  SER   BBB O   1 ? 
ATOM   2709 C  CB  . SER   B 1 86  ? 43.850  42.907 71.366 1.000 45.004  ? 85  SER   BBB CB  1 ? 
ATOM   2710 O  OG  . SER   B 1 86  ? 44.305  42.041 70.342 1.000 51.614  ? 85  SER   BBB OG  1 ? 
ATOM   2711 N  N   . ASP   B 1 87  ? 42.101  43.848 68.655 1.000 44.501  ? 86  ASP   BBB N   1 ? 
ATOM   2712 C  CA  . ASP   B 1 87  ? 42.037  44.584 67.365 1.000 45.833  ? 86  ASP   BBB CA  1 ? 
ATOM   2713 C  C   . ASP   B 1 87  ? 40.622  45.125 67.152 1.000 38.435  ? 86  ASP   BBB C   1 ? 
ATOM   2714 O  O   . ASP   B 1 87  ? 39.655  44.501 67.648 1.000 39.040  ? 86  ASP   BBB O   1 ? 
ATOM   2715 C  CB  . ASP   B 1 87  ? 42.350  43.662 66.179 1.000 49.990  ? 86  ASP   BBB CB  1 ? 
ATOM   2716 C  CG  . ASP   B 1 87  ? 43.728  43.023 66.201 1.000 56.021  ? 86  ASP   BBB CG  1 ? 
ATOM   2717 O  OD1 . ASP   B 1 87  ? 44.670  43.679 66.676 1.000 56.674  ? 86  ASP   BBB OD1 1 ? 
ATOM   2718 O  OD2 . ASP   B 1 87  ? 43.839  41.857 65.733 1.000 62.737  ? 86  ASP   BBB OD2 1 ? 
ATOM   2719 N  N   . SER   B 1 88  ? 40.483  46.219 66.413 1.000 39.343  ? 87  SER   BBB N   1 ? 
ATOM   2720 C  CA  . SER   B 1 88  ? 39.167  46.679 65.900 1.000 40.670  ? 87  SER   BBB CA  1 ? 
ATOM   2721 C  C   . SER   B 1 88  ? 38.847  45.940 64.601 1.000 30.761  ? 87  SER   BBB C   1 ? 
ATOM   2722 O  O   . SER   B 1 88  ? 39.759  45.732 63.763 1.000 33.121  ? 87  SER   BBB O   1 ? 
ATOM   2723 C  CB  . SER   B 1 88  ? 39.142  48.169 65.718 1.000 44.157  ? 87  SER   BBB CB  1 ? 
ATOM   2724 O  OG  . SER   B 1 88  ? 39.084  48.778 67.017 1.000 48.937  ? 87  SER   BBB OG  1 ? 
ATOM   2725 N  N   . TYR   B 1 89  ? 37.578  45.566 64.431 1.000 28.887  ? 88  TYR   BBB N   1 ? 
ATOM   2726 C  CA  . TYR   B 1 89  ? 37.063  44.910 63.212 1.000 28.725  ? 88  TYR   BBB CA  1 ? 
ATOM   2727 C  C   . TYR   B 1 89  ? 36.116  45.862 62.483 1.000 26.828  ? 88  TYR   BBB C   1 ? 
ATOM   2728 O  O   . TYR   B 1 89  ? 35.226  46.443 63.102 1.000 27.618  ? 88  TYR   BBB O   1 ? 
ATOM   2729 C  CB  . TYR   B 1 89  ? 36.362  43.611 63.605 1.000 27.659  ? 88  TYR   BBB CB  1 ? 
ATOM   2730 C  CG  . TYR   B 1 89  ? 37.303  42.494 63.997 1.000 28.134  ? 88  TYR   BBB CG  1 ? 
ATOM   2731 C  CD1 . TYR   B 1 89  ? 38.029  42.546 65.173 1.000 30.346  ? 88  TYR   BBB CD1 1 ? 
ATOM   2732 C  CD2 . TYR   B 1 89  ? 37.415  41.355 63.218 1.000 28.209  ? 88  TYR   BBB CD2 1 ? 
ATOM   2733 C  CE1 . TYR   B 1 89  ? 38.871  41.518 65.556 1.000 29.854  ? 88  TYR   BBB CE1 1 ? 
ATOM   2734 C  CE2 . TYR   B 1 89  ? 38.259  40.311 63.587 1.000 27.277  ? 88  TYR   BBB CE2 1 ? 
ATOM   2735 C  CZ  . TYR   B 1 89  ? 39.009  40.411 64.738 1.000 31.087  ? 88  TYR   BBB CZ  1 ? 
ATOM   2736 O  OH  . TYR   B 1 89  ? 39.864  39.404 65.074 1.000 35.318  ? 88  TYR   BBB OH  1 ? 
ATOM   2737 N  N   . ARG   B 1 90  ? 36.253  45.899 61.167 1.000 28.946  ? 89  ARG   BBB N   1 ? 
ATOM   2738 C  CA  . ARG   B 1 90  ? 35.485  46.806 60.281 1.000 29.143  ? 89  ARG   BBB CA  1 ? 
ATOM   2739 C  C   . ARG   B 1 90  ? 34.171  46.144 59.850 1.000 25.489  ? 89  ARG   BBB C   1 ? 
ATOM   2740 O  O   . ARG   B 1 90  ? 34.223  45.079 59.226 1.000 25.694  ? 89  ARG   BBB O   1 ? 
ATOM   2741 C  CB  . ARG   B 1 90  ? 36.337  47.130 59.055 1.000 34.001  ? 89  ARG   BBB CB  1 ? 
ATOM   2742 C  CG  . ARG   B 1 90  ? 35.770  48.225 58.168 1.000 35.296  ? 89  ARG   BBB CG  1 ? 
ATOM   2743 C  CD  . ARG   B 1 90  ? 36.797  48.660 57.120 1.000 40.031  ? 89  ARG   BBB CD  1 ? 
ATOM   2744 N  NE  . ARG   B 1 90  ? 38.068  49.138 57.663 1.000 49.222  ? 89  ARG   BBB NE  1 ? 
ATOM   2745 C  CZ  . ARG   B 1 90  ? 39.155  49.447 56.937 1.000 43.202  ? 89  ARG   BBB CZ  1 ? 
ATOM   2746 N  NH1 . ARG   B 1 90  ? 39.158  49.326 55.621 1.000 42.314  ? 89  ARG   BBB NH1 1 ? 
ATOM   2747 N  NH2 . ARG   B 1 90  ? 40.245  49.884 57.533 1.000 61.906  ? 89  ARG   BBB NH2 1 ? 
ATOM   2748 N  N   . LEU   B 1 91  ? 33.051  46.806 60.112 1.000 24.459  ? 90  LEU   BBB N   1 ? 
ATOM   2749 C  CA  . LEU   B 1 91  ? 31.700  46.445 59.624 1.000 23.658  ? 90  LEU   BBB CA  1 ? 
ATOM   2750 C  C   . LEU   B 1 91  ? 31.709  46.362 58.105 1.000 21.171  ? 90  LEU   BBB C   1 ? 
ATOM   2751 O  O   . LEU   B 1 91  ? 32.211  47.285 57.430 1.000 22.622  ? 90  LEU   BBB O   1 ? 
ATOM   2752 C  CB  . LEU   B 1 91  ? 30.649  47.454 60.109 1.000 23.268  ? 90  LEU   BBB CB  1 ? 
ATOM   2753 C  CG  . LEU   B 1 91  ? 29.240  47.268 59.553 1.000 25.768  ? 90  LEU   BBB CG  1 ? 
ATOM   2754 C  CD1 . LEU   B 1 91  ? 28.619  45.927 60.088 1.000 26.544  ? 90  LEU   BBB CD1 1 ? 
ATOM   2755 C  CD2 . LEU   B 1 91  ? 28.340  48.444 59.866 1.000 27.739  ? 90  LEU   BBB CD2 1 ? 
ATOM   2756 N  N   . PHE   B 1 92  ? 31.161  45.268 57.544 1.000 21.769  ? 91  PHE   BBB N   1 ? 
ATOM   2757 C  CA  . PHE   B 1 92  ? 31.026  45.170 56.062 1.000 21.423  ? 91  PHE   BBB CA  1 ? 
ATOM   2758 C  C   . PHE   B 1 92  ? 29.603  44.757 55.648 1.000 17.728  ? 91  PHE   BBB C   1 ? 
ATOM   2759 O  O   . PHE   B 1 92  ? 29.224  45.071 54.494 1.000 21.791  ? 91  PHE   BBB O   1 ? 
ATOM   2760 C  CB  . PHE   B 1 92  ? 32.174  44.346 55.452 1.000 21.954  ? 91  PHE   BBB CB  1 ? 
ATOM   2761 C  CG  . PHE   B 1 92  ? 32.142  42.848 55.678 1.000 20.615  ? 91  PHE   BBB CG  1 ? 
ATOM   2762 C  CD1 . PHE   B 1 92  ? 32.775  42.278 56.771 1.000 21.668  ? 91  PHE   BBB CD1 1 ? 
ATOM   2763 C  CD2 . PHE   B 1 92  ? 31.504  42.037 54.760 1.000 19.988  ? 91  PHE   BBB CD2 1 ? 
ATOM   2764 C  CE1 . PHE   B 1 92  ? 32.752  40.900 56.956 1.000 22.119  ? 91  PHE   BBB CE1 1 ? 
ATOM   2765 C  CE2 . PHE   B 1 92  ? 31.478  40.643 54.932 1.000 21.520  ? 91  PHE   BBB CE2 1 ? 
ATOM   2766 C  CZ  . PHE   B 1 92  ? 32.113  40.111 56.021 1.000 21.928  ? 91  PHE   BBB CZ  1 ? 
ATOM   2767 N  N   . GLN   B 1 93  ? 28.845  44.053 56.493 1.000 18.238  ? 92  GLN   BBB N   1 ? 
ATOM   2768 C  CA  . GLN   B 1 93  ? 27.545  43.498 56.037 1.000 18.610  ? 92  GLN   BBB CA  1 ? 
ATOM   2769 C  C   . GLN   B 1 93  ? 26.671  43.153 57.237 1.000 18.589  ? 92  GLN   BBB C   1 ? 
ATOM   2770 O  O   . GLN   B 1 93  ? 27.233  42.790 58.301 1.000 18.905  ? 92  GLN   BBB O   1 ? 
ATOM   2771 C  CB  . GLN   B 1 93  ? 27.807  42.201 55.246 1.000 21.483  ? 92  GLN   BBB CB  1 ? 
ATOM   2772 C  CG  . GLN   B 1 93  ? 26.574  41.529 54.674 1.000 23.790  ? 92  GLN   BBB CG  1 ? 
ATOM   2773 C  CD  . GLN   B 1 93  ? 26.960  40.303 53.888 1.000 22.627  ? 92  GLN   BBB CD  1 ? 
ATOM   2774 O  OE1 . GLN   B 1 93  ? 26.724  39.184 54.353 1.000 21.996  ? 92  GLN   BBB OE1 1 ? 
ATOM   2775 N  NE2 . GLN   B 1 93  ? 27.567  40.515 52.713 1.000 23.945  ? 92  GLN   BBB NE2 1 ? 
ATOM   2776 N  N   . PHE   B 1 94  ? 25.354  43.224 57.078 1.000 20.121  ? 93  PHE   BBB N   1 ? 
ATOM   2777 C  CA  . PHE   B 1 94  ? 24.465  42.367 57.919 1.000 16.929  ? 93  PHE   BBB CA  1 ? 
ATOM   2778 C  C   . PHE   B 1 94  ? 23.421  41.688 57.050 1.000 16.883  ? 93  PHE   BBB C   1 ? 
ATOM   2779 O  O   . PHE   B 1 94  ? 23.232  41.989 55.855 1.000 18.438  ? 93  PHE   BBB O   1 ? 
ATOM   2780 C  CB  . PHE   B 1 94  ? 23.816  43.161 59.055 1.000 17.710  ? 93  PHE   BBB CB  1 ? 
ATOM   2781 C  CG  . PHE   B 1 94  ? 22.702  44.066 58.595 1.000 18.133  ? 93  PHE   BBB CG  1 ? 
ATOM   2782 C  CD1 . PHE   B 1 94  ? 21.416  43.617 58.495 1.000 20.478  ? 93  PHE   BBB CD1 1 ? 
ATOM   2783 C  CD2 . PHE   B 1 94  ? 22.915  45.437 58.404 1.000 19.361  ? 93  PHE   BBB CD2 1 ? 
ATOM   2784 C  CE1 . PHE   B 1 94  ? 20.350  44.423 58.154 1.000 18.523  ? 93  PHE   BBB CE1 1 ? 
ATOM   2785 C  CE2 . PHE   B 1 94  ? 21.859  46.238 58.014 1.000 20.159  ? 93  PHE   BBB CE2 1 ? 
ATOM   2786 C  CZ  . PHE   B 1 94  ? 20.572  45.781 57.951 1.000 21.074  ? 93  PHE   BBB CZ  1 ? 
ATOM   2787 N  N   . HIS   B 1 95  ? 22.940  40.555 57.608 1.000 19.535  ? 94  HIS   BBB N   1 ? 
ATOM   2788 C  CA  . HIS   B 1 95  ? 21.934  39.745 56.896 1.000 17.966  ? 94  HIS   BBB CA  1 ? 
ATOM   2789 C  C   . HIS   B 1 95  ? 21.208  38.904 57.936 1.000 17.489  ? 94  HIS   BBB C   1 ? 
ATOM   2790 O  O   . HIS   B 1 95  ? 21.531  38.975 59.119 1.000 20.759  ? 94  HIS   BBB O   1 ? 
ATOM   2791 C  CB  . HIS   B 1 95  ? 22.586  38.873 55.804 1.000 17.711  ? 94  HIS   BBB CB  1 ? 
ATOM   2792 C  CG  . HIS   B 1 95  ? 23.555  37.888 56.376 1.000 18.023  ? 94  HIS   BBB CG  1 ? 
ATOM   2793 N  ND1 . HIS   B 1 95  ? 24.906  38.013 56.243 1.000 19.895  ? 94  HIS   BBB ND1 1 ? 
ATOM   2794 C  CD2 . HIS   B 1 95  ? 23.350  36.706 57.054 1.000 20.744  ? 94  HIS   BBB CD2 1 ? 
ATOM   2795 C  CE1 . HIS   B 1 95  ? 25.522  36.955 56.810 1.000 21.198  ? 94  HIS   BBB CE1 1 ? 
ATOM   2796 N  NE2 . HIS   B 1 95  ? 24.584  36.208 57.422 1.000 31.468  ? 94  HIS   BBB NE2 1 ? 
ATOM   2797 N  N   . PHE   B 1 96  ? 20.237  38.127 57.430 1.000 14.947  ? 95  PHE   BBB N   1 ? 
ATOM   2798 C  CA  . PHE   B 1 96  ? 19.382  37.296 58.297 1.000 15.959  ? 95  PHE   BBB CA  1 ? 
ATOM   2799 C  C   . PHE   B 1 96  ? 19.429  35.849 57.784 1.000 18.352  ? 95  PHE   BBB C   1 ? 
ATOM   2800 O  O   . PHE   B 1 96  ? 19.742  35.656 56.619 1.000 18.057  ? 95  PHE   BBB O   1 ? 
ATOM   2801 C  CB  . PHE   B 1 96  ? 17.952  37.794 58.373 1.000 16.802  ? 95  PHE   BBB CB  1 ? 
ATOM   2802 C  CG  . PHE   B 1 96  ? 17.852  39.229 58.836 1.000 17.818  ? 95  PHE   BBB CG  1 ? 
ATOM   2803 C  CD1 . PHE   B 1 96  ? 17.989  40.223 57.894 1.000 18.191  ? 95  PHE   BBB CD1 1 ? 
ATOM   2804 C  CD2 . PHE   B 1 96  ? 17.583  39.559 60.152 1.000 17.168  ? 95  PHE   BBB CD2 1 ? 
ATOM   2805 C  CE1 . PHE   B 1 96  ? 17.895  41.554 58.292 1.000 18.296  ? 95  PHE   BBB CE1 1 ? 
ATOM   2806 C  CE2 . PHE   B 1 96  ? 17.464  40.887 60.544 1.000 18.602  ? 95  PHE   BBB CE2 1 ? 
ATOM   2807 C  CZ  . PHE   B 1 96  ? 17.671  41.864 59.608 1.000 19.928  ? 95  PHE   BBB CZ  1 ? 
ATOM   2808 N  N   . HIS   B 1 97  ? 19.020  34.969 58.667 1.000 17.124  ? 96  HIS   BBB N   1 ? 
ATOM   2809 C  CA  . HIS   B 1 97  ? 18.631  33.568 58.332 1.000 16.599  ? 96  HIS   BBB CA  1 ? 
ATOM   2810 C  C   . HIS   B 1 97  ? 17.237  33.380 58.876 1.000 17.729  ? 96  HIS   BBB C   1 ? 
ATOM   2811 O  O   . HIS   B 1 97  ? 16.894  33.868 59.985 1.000 18.312  ? 96  HIS   BBB O   1 ? 
ATOM   2812 C  CB  . HIS   B 1 97  ? 19.630  32.549 58.867 1.000 16.516  ? 96  HIS   BBB CB  1 ? 
ATOM   2813 C  CG  . HIS   B 1 97  ? 21.015  32.706 58.379 1.000 16.244  ? 96  HIS   BBB CG  1 ? 
ATOM   2814 N  ND1 . HIS   B 1 97  ? 21.559  31.990 57.304 1.000 19.893  ? 96  HIS   BBB ND1 1 ? 
ATOM   2815 C  CD2 . HIS   B 1 97  ? 22.002  33.550 58.783 1.000 17.786  ? 96  HIS   BBB CD2 1 ? 
ATOM   2816 C  CE1 . HIS   B 1 97  ? 22.796  32.397 57.102 1.000 17.824  ? 96  HIS   BBB CE1 1 ? 
ATOM   2817 N  NE2 . HIS   B 1 97  ? 23.089  33.309 58.031 1.000 16.482  ? 96  HIS   BBB NE2 1 ? 
ATOM   2818 N  N   . TRP   B 1 98  ? 16.491  32.520 58.194 1.000 18.110  ? 97  TRP   BBB N   1 ? 
ATOM   2819 C  CA  . TRP   B 1 98  ? 15.149  32.149 58.637 1.000 18.842  ? 97  TRP   BBB CA  1 ? 
ATOM   2820 C  C   . TRP   B 1 98  ? 14.880  30.718 58.193 1.000 20.004  ? 97  TRP   BBB C   1 ? 
ATOM   2821 O  O   . TRP   B 1 98  ? 15.700  30.190 57.406 1.000 19.586  ? 97  TRP   BBB O   1 ? 
ATOM   2822 C  CB  . TRP   B 1 98  ? 14.132  33.158 58.088 1.000 16.682  ? 97  TRP   BBB CB  1 ? 
ATOM   2823 C  CG  . TRP   B 1 98  ? 14.124  33.249 56.601 1.000 17.469  ? 97  TRP   BBB CG  1 ? 
ATOM   2824 C  CD1 . TRP   B 1 98  ? 13.393  32.509 55.720 1.000 18.916  ? 97  TRP   BBB CD1 1 ? 
ATOM   2825 C  CD2 . TRP   B 1 98  ? 14.895  34.159 55.808 1.000 18.222  ? 97  TRP   BBB CD2 1 ? 
ATOM   2826 N  NE1 . TRP   B 1 98  ? 13.672  32.872 54.432 1.000 19.642  ? 97  TRP   BBB NE1 1 ? 
ATOM   2827 C  CE2 . TRP   B 1 98  ? 14.541  33.940 54.464 1.000 17.502  ? 97  TRP   BBB CE2 1 ? 
ATOM   2828 C  CE3 . TRP   B 1 98  ? 15.733  35.240 56.119 1.000 18.001  ? 97  TRP   BBB CE3 1 ? 
ATOM   2829 C  CZ2 . TRP   B 1 98  ? 15.102  34.678 53.423 1.000 19.126  ? 97  TRP   BBB CZ2 1 ? 
ATOM   2830 C  CZ3 . TRP   B 1 98  ? 16.322  35.926 55.078 1.000 19.040  ? 97  TRP   BBB CZ3 1 ? 
ATOM   2831 C  CH2 . TRP   B 1 98  ? 15.965  35.710 53.763 1.000 17.007  ? 97  TRP   BBB CH2 1 ? 
ATOM   2832 N  N   . GLY   B 1 99  ? 13.728  30.237 58.609 1.000 19.774  ? 98  GLY   BBB N   1 ? 
ATOM   2833 C  CA  . GLY   B 1 99  ? 13.371  28.827 58.347 1.000 22.154  ? 98  GLY   BBB CA  1 ? 
ATOM   2834 C  C   . GLY   B 1 99  ? 12.048  28.724 57.625 1.000 20.791  ? 98  GLY   BBB C   1 ? 
ATOM   2835 O  O   . GLY   B 1 99  ? 11.310  29.710 57.461 1.000 21.668  ? 98  GLY   BBB O   1 ? 
ATOM   2836 N  N   . SER   B 1 100 ? 11.655  27.534 57.222 1.000 25.230  ? 99  SER   BBB N   1 ? 
ATOM   2837 C  CA  A SER   B 1 100 ? 10.409  27.378 56.435 0.500 25.250  ? 99  SER   BBB CA  1 ? 
ATOM   2838 C  CA  B SER   B 1 100 ? 10.405  27.328 56.450 0.500 25.329  ? 99  SER   BBB CA  1 ? 
ATOM   2839 C  C   . SER   B 1 100 ? 9.191   27.645 57.332 1.000 24.728  ? 99  SER   BBB C   1 ? 
ATOM   2840 O  O   . SER   B 1 100 ? 8.135   27.951 56.783 1.000 29.590  ? 99  SER   BBB O   1 ? 
ATOM   2841 C  CB  A SER   B 1 100 ? 10.345  26.010 55.796 0.500 26.733  ? 99  SER   BBB CB  1 ? 
ATOM   2842 C  CB  B SER   B 1 100 ? 10.312  25.902 55.963 0.500 28.480  ? 99  SER   BBB CB  1 ? 
ATOM   2843 O  OG  A SER   B 1 100 ? 10.472  24.978 56.764 0.500 31.553  ? 99  SER   BBB OG  1 ? 
ATOM   2844 O  OG  B SER   B 1 100 ? 11.435  25.528 55.170 0.500 30.943  ? 99  SER   BBB OG  1 ? 
ATOM   2845 N  N   . THR   B 1 101 ? 9.329   27.488 58.656 1.000 24.264  ? 100 THR   BBB N   1 ? 
ATOM   2846 C  CA  . THR   B 1 101 ? 8.255   27.752 59.654 1.000 29.266  ? 100 THR   BBB CA  1 ? 
ATOM   2847 C  C   . THR   B 1 101 ? 8.821   28.657 60.742 1.000 28.816  ? 100 THR   BBB C   1 ? 
ATOM   2848 O  O   . THR   B 1 101 ? 10.074  28.741 60.858 1.000 30.005  ? 100 THR   BBB O   1 ? 
ATOM   2849 C  CB  . THR   B 1 101 ? 7.708   26.475 60.316 1.000 33.181  ? 100 THR   BBB CB  1 ? 
ATOM   2850 O  OG1 . THR   B 1 101 ? 8.677   26.052 61.284 1.000 37.275  ? 100 THR   BBB OG1 1 ? 
ATOM   2851 C  CG2 . THR   B 1 101 ? 7.419   25.332 59.359 1.000 33.785  ? 100 THR   BBB CG2 1 ? 
ATOM   2852 N  N   . ASN   B 1 102 ? 7.947   29.232 61.566 1.000 28.498  ? 101 ASN   BBB N   1 ? 
ATOM   2853 C  CA  . ASN   B 1 102 ? 8.389   30.081 62.713 1.000 30.392  ? 101 ASN   BBB CA  1 ? 
ATOM   2854 C  C   . ASN   B 1 102 ? 9.088   29.240 63.803 1.000 30.362  ? 101 ASN   BBB C   1 ? 
ATOM   2855 O  O   . ASN   B 1 102 ? 9.895   29.781 64.542 1.000 33.414  ? 101 ASN   BBB O   1 ? 
ATOM   2856 C  CB  . ASN   B 1 102 ? 7.202   30.846 63.281 1.000 33.817  ? 101 ASN   BBB CB  1 ? 
ATOM   2857 C  CG  . ASN   B 1 102 ? 6.551   31.799 62.256 1.000 34.087  ? 101 ASN   BBB CG  1 ? 
ATOM   2858 O  OD1 . ASN   B 1 102 ? 7.096   32.103 61.182 1.000 35.729  ? 101 ASN   BBB OD1 1 ? 
ATOM   2859 N  ND2 . ASN   B 1 102 ? 5.336   32.194 62.564 1.000 35.443  ? 101 ASN   BBB ND2 1 ? 
ATOM   2860 N  N   . GLU   B 1 103 ? 8.850   27.932 63.874 1.000 35.033  ? 102 GLU   BBB N   1 ? 
ATOM   2861 C  CA  . GLU   B 1 103 ? 9.391   27.029 64.942 1.000 38.457  ? 102 GLU   BBB CA  1 ? 
ATOM   2862 C  C   . GLU   B 1 103 ? 10.913  26.837 64.815 1.000 35.388  ? 102 GLU   BBB C   1 ? 
ATOM   2863 O  O   . GLU   B 1 103 ? 11.527  26.401 65.814 1.000 38.701  ? 102 GLU   BBB O   1 ? 
ATOM   2864 C  CB  . GLU   B 1 103 ? 8.676   25.669 64.912 1.000 38.611  ? 102 GLU   BBB CB  1 ? 
ATOM   2865 C  CG  . GLU   B 1 103 ? 7.218   25.748 65.349 1.000 55.792  ? 102 GLU   BBB CG  1 ? 
ATOM   2866 C  CD  . GLU   B 1 103 ? 6.285   26.439 64.360 1.000 59.059  ? 102 GLU   BBB CD  1 ? 
ATOM   2867 O  OE1 . GLU   B 1 103 ? 6.244   26.009 63.183 1.000 81.074  ? 102 GLU   BBB OE1 1 ? 
ATOM   2868 O  OE2 . GLU   B 1 103 ? 5.632   27.434 64.754 1.000 82.567  ? 102 GLU   BBB OE2 1 ? 
ATOM   2869 N  N   . HIS   B 1 104 ? 11.536  27.151 63.669 1.000 26.721  ? 103 HIS   BBB N   1 ? 
ATOM   2870 C  CA  . HIS   B 1 104 ? 13.005  26.986 63.521 1.000 28.402  ? 103 HIS   BBB CA  1 ? 
ATOM   2871 C  C   . HIS   B 1 104 ? 13.477  27.671 62.262 1.000 29.167  ? 103 HIS   BBB C   1 ? 
ATOM   2872 O  O   . HIS   B 1 104 ? 13.318  27.152 61.138 1.000 34.602  ? 103 HIS   BBB O   1 ? 
ATOM   2873 C  CB  . HIS   B 1 104 ? 13.537  25.524 63.442 1.000 36.262  ? 103 HIS   BBB CB  1 ? 
ATOM   2874 C  CG  . HIS   B 1 104 ? 15.061  25.415 63.424 1.000 52.392  ? 103 HIS   BBB CG  1 ? 
ATOM   2875 N  ND1 . HIS   B 1 104 ? 15.746  24.318 62.874 1.000 65.569  ? 103 HIS   BBB ND1 1 ? 
ATOM   2876 C  CD2 . HIS   B 1 104 ? 16.055  26.243 63.866 1.000 47.435  ? 103 HIS   BBB CD2 1 ? 
ATOM   2877 C  CE1 . HIS   B 1 104 ? 17.064  24.483 62.995 1.000 56.774  ? 103 HIS   BBB CE1 1 ? 
ATOM   2878 N  NE2 . HIS   B 1 104 ? 17.285  25.657 63.596 1.000 46.246  ? 103 HIS   BBB NE2 1 ? 
ATOM   2879 N  N   . GLY   B 1 105 ? 14.132  28.774 62.506 1.000 23.609  ? 104 GLY   BBB N   1 ? 
ATOM   2880 C  CA  . GLY   B 1 105 ? 14.825  29.528 61.464 1.000 23.368  ? 104 GLY   BBB CA  1 ? 
ATOM   2881 C  C   . GLY   B 1 105 ? 16.139  30.051 61.970 1.000 18.497  ? 104 GLY   BBB C   1 ? 
ATOM   2882 O  O   . GLY   B 1 105 ? 16.887  30.504 61.078 1.000 21.667  ? 104 GLY   BBB O   1 ? 
ATOM   2883 N  N   . SER   B 1 106 ? 16.449  29.990 63.274 1.000 17.429  ? 105 SER   BBB N   1 ? 
ATOM   2884 C  CA  . SER   B 1 106 ? 17.786  30.453 63.724 1.000 18.257  ? 105 SER   BBB CA  1 ? 
ATOM   2885 C  C   . SER   B 1 106 ? 18.837  29.423 63.275 1.000 18.177  ? 105 SER   BBB C   1 ? 
ATOM   2886 O  O   . SER   B 1 106 ? 18.516  28.210 62.868 1.000 20.269  ? 105 SER   BBB O   1 ? 
ATOM   2887 C  CB  . SER   B 1 106 ? 17.900  30.740 65.201 1.000 17.581  ? 105 SER   BBB CB  1 ? 
ATOM   2888 O  OG  . SER   B 1 106 ? 17.793  29.518 65.939 1.000 23.664  ? 105 SER   BBB OG  1 ? 
ATOM   2889 N  N   . GLU   B 1 107 ? 20.098  29.812 63.369 1.000 17.416  ? 106 GLU   BBB N   1 ? 
ATOM   2890 C  CA  . GLU   B 1 107 ? 21.245  28.924 63.064 1.000 19.668  ? 106 GLU   BBB CA  1 ? 
ATOM   2891 C  C   . GLU   B 1 107 ? 21.775  28.469 64.408 1.000 20.627  ? 106 GLU   BBB C   1 ? 
ATOM   2892 O  O   . GLU   B 1 107 ? 21.708  27.202 64.680 1.000 20.224  ? 106 GLU   BBB O   1 ? 
ATOM   2893 C  CB  . GLU   B 1 107 ? 22.282  29.627 62.188 1.000 19.459  ? 106 GLU   BBB CB  1 ? 
ATOM   2894 C  CG  . GLU   B 1 107 ? 21.783  29.861 60.783 1.000 20.495  ? 106 GLU   BBB CG  1 ? 
ATOM   2895 C  CD  . GLU   B 1 107 ? 22.848  29.932 59.741 1.000 16.755  ? 106 GLU   BBB CD  1 ? 
ATOM   2896 O  OE1 . GLU   B 1 107 ? 22.686  29.294 58.687 1.000 21.085  ? 106 GLU   BBB OE1 1 ? 
ATOM   2897 O  OE2 . GLU   B 1 107 ? 23.786  30.861 59.914 1.000 22.248  ? 106 GLU   BBB OE2 1 ? 
ATOM   2898 N  N   . HIS   B 1 108 ? 22.256  29.339 65.263 1.000 18.503  ? 107 HIS   BBB N   1 ? 
ATOM   2899 C  CA  . HIS   B 1 108 ? 22.587  29.004 66.656 1.000 18.487  ? 107 HIS   BBB CA  1 ? 
ATOM   2900 C  C   . HIS   B 1 108 ? 21.327  28.622 67.432 1.000 20.602  ? 107 HIS   BBB C   1 ? 
ATOM   2901 O  O   . HIS   B 1 108 ? 20.188  29.009 67.063 1.000 23.203  ? 107 HIS   BBB O   1 ? 
ATOM   2902 C  CB  . HIS   B 1 108 ? 23.389  30.125 67.317 1.000 19.889  ? 107 HIS   BBB CB  1 ? 
ATOM   2903 C  CG  . HIS   B 1 108 ? 24.707  30.341 66.676 1.000 18.117  ? 107 HIS   BBB CG  1 ? 
ATOM   2904 N  ND1 . HIS   B 1 108 ? 24.885  31.185 65.588 1.000 21.975  ? 107 HIS   BBB ND1 1 ? 
ATOM   2905 C  CD2 . HIS   B 1 108 ? 25.932  29.808 66.954 1.000 19.708  ? 107 HIS   BBB CD2 1 ? 
ATOM   2906 C  CE1 . HIS   B 1 108 ? 26.148  31.127 65.229 1.000 23.537  ? 107 HIS   BBB CE1 1 ? 
ATOM   2907 N  NE2 . HIS   B 1 108 ? 26.824  30.255 66.029 1.000 20.245  ? 107 HIS   BBB NE2 1 ? 
ATOM   2908 N  N   . THR   B 1 109 ? 21.533  27.639 68.345 1.000 23.602  ? 108 THR   BBB N   1 ? 
ATOM   2909 C  CA  . THR   B 1 109 ? 20.497  27.273 69.335 1.000 24.438  ? 108 THR   BBB CA  1 ? 
ATOM   2910 C  C   . THR   B 1 109 ? 21.094  27.378 70.732 1.000 22.300  ? 108 THR   BBB C   1 ? 
ATOM   2911 O  O   . THR   B 1 109 ? 22.296  27.419 70.845 1.000 21.503  ? 108 THR   BBB O   1 ? 
ATOM   2912 C  CB  . THR   B 1 109 ? 19.987  25.841 69.078 1.000 22.516  ? 108 THR   BBB CB  1 ? 
ATOM   2913 O  OG1 . THR   B 1 109 ? 21.101  24.953 69.218 1.000 22.277  ? 108 THR   BBB OG1 1 ? 
ATOM   2914 C  CG2 . THR   B 1 109 ? 19.380  25.735 67.696 1.000 24.220  ? 108 THR   BBB CG2 1 ? 
ATOM   2915 N  N   . VAL   B 1 110 ? 20.216  27.507 71.717 1.000 21.000  ? 109 VAL   BBB N   1 ? 
ATOM   2916 C  CA  . VAL   B 1 110 ? 20.627  27.661 73.160 1.000 21.060  ? 109 VAL   BBB CA  1 ? 
ATOM   2917 C  C   . VAL   B 1 110 ? 19.879  26.620 73.962 1.000 21.868  ? 109 VAL   BBB C   1 ? 
ATOM   2918 O  O   . VAL   B 1 110 ? 18.634  26.660 73.953 1.000 21.846  ? 109 VAL   BBB O   1 ? 
ATOM   2919 C  CB  . VAL   B 1 110 ? 20.354  29.080 73.678 1.000 20.524  ? 109 VAL   BBB CB  1 ? 
ATOM   2920 C  CG1 . VAL   B 1 110 ? 20.805  29.251 75.116 1.000 25.506  ? 109 VAL   BBB CG1 1 ? 
ATOM   2921 C  CG2 . VAL   B 1 110 ? 21.030  30.091 72.811 1.000 21.920  ? 109 VAL   BBB CG2 1 ? 
ATOM   2922 N  N   . ASP   B 1 111 ? 20.649  25.691 74.539 1.000 21.683  ? 110 ASP   BBB N   1 ? 
ATOM   2923 C  CA  . ASP   B 1 111 ? 20.090  24.502 75.244 1.000 22.714  ? 110 ASP   BBB CA  1 ? 
ATOM   2924 C  C   . ASP   B 1 111 ? 19.042  23.807 74.352 1.000 22.810  ? 110 ASP   BBB C   1 ? 
ATOM   2925 O  O   . ASP   B 1 111 ? 17.961  23.404 74.856 1.000 26.333  ? 110 ASP   BBB O   1 ? 
ATOM   2926 C  CB  . ASP   B 1 111 ? 19.529  24.914 76.606 1.000 23.441  ? 110 ASP   BBB CB  1 ? 
ATOM   2927 C  CG  . ASP   B 1 111 ? 20.580  25.435 77.568 1.000 24.157  ? 110 ASP   BBB CG  1 ? 
ATOM   2928 O  OD1 . ASP   B 1 111 ? 21.670  24.828 77.636 1.000 30.045  ? 110 ASP   BBB OD1 1 ? 
ATOM   2929 O  OD2 . ASP   B 1 111 ? 20.330  26.503 78.201 1.000 27.316  ? 110 ASP   BBB OD2 1 ? 
ATOM   2930 N  N   . GLY   B 1 112 ? 19.376  23.647 73.068 1.000 23.608  ? 111 GLY   BBB N   1 ? 
ATOM   2931 C  CA  . GLY   B 1 112 ? 18.534  22.959 72.069 1.000 27.996  ? 111 GLY   BBB CA  1 ? 
ATOM   2932 C  C   . GLY   B 1 112 ? 17.328  23.756 71.597 1.000 30.018  ? 111 GLY   BBB C   1 ? 
ATOM   2933 O  O   . GLY   B 1 112 ? 16.591  23.238 70.718 1.000 29.550  ? 111 GLY   BBB O   1 ? 
ATOM   2934 N  N   . VAL   B 1 113 ? 17.160  25.008 72.050 1.000 26.935  ? 112 VAL   BBB N   1 ? 
ATOM   2935 C  CA  . VAL   B 1 113 ? 15.955  25.813 71.710 1.000 25.372  ? 112 VAL   BBB CA  1 ? 
ATOM   2936 C  C   . VAL   B 1 113 ? 16.252  26.521 70.381 1.000 22.754  ? 112 VAL   BBB C   1 ? 
ATOM   2937 O  O   . VAL   B 1 113 ? 17.338  27.200 70.264 1.000 23.538  ? 112 VAL   BBB O   1 ? 
ATOM   2938 C  CB  . VAL   B 1 113 ? 15.580  26.812 72.813 1.000 27.233  ? 112 VAL   BBB CB  1 ? 
ATOM   2939 C  CG1 . VAL   B 1 113 ? 14.485  27.773 72.342 1.000 28.824  ? 112 VAL   BBB CG1 1 ? 
ATOM   2940 C  CG2 . VAL   B 1 113 ? 15.160  26.169 74.115 1.000 27.497  ? 112 VAL   BBB CG2 1 ? 
ATOM   2941 N  N   . LYS   B 1 114 ? 15.383  26.333 69.401 1.000 23.907  ? 113 LYS   BBB N   1 ? 
ATOM   2942 C  CA  . LYS   B 1 114 ? 15.536  26.917 68.047 1.000 23.600  ? 113 LYS   BBB CA  1 ? 
ATOM   2943 C  C   . LYS   B 1 114 ? 14.678  28.171 68.005 1.000 23.462  ? 113 LYS   BBB C   1 ? 
ATOM   2944 O  O   . LYS   B 1 114 ? 13.527  28.107 68.391 1.000 27.889  ? 113 LYS   BBB O   1 ? 
ATOM   2945 C  CB  . LYS   B 1 114 ? 15.093  25.929 66.970 1.000 29.754  ? 113 LYS   BBB CB  1 ? 
ATOM   2946 C  CG  . LYS   B 1 114 ? 15.885  24.641 66.996 1.000 32.677  ? 113 LYS   BBB CG  1 ? 
ATOM   2947 C  CD  . LYS   B 1 114 ? 15.256  23.427 66.349 1.000 44.102  ? 113 LYS   BBB CD  1 ? 
ATOM   2948 C  CE  . LYS   B 1 114 ? 16.287  22.328 66.234 1.000 62.600  ? 113 LYS   BBB CE  1 ? 
ATOM   2949 N  NZ  . LYS   B 1 114 ? 15.678  21.149 65.598 1.000 66.208  ? 113 LYS   BBB NZ  1 ? 
ATOM   2950 N  N   . TYR   B 1 115 ? 15.254  29.283 67.591 1.000 20.757  ? 114 TYR   BBB N   1 ? 
ATOM   2951 C  CA  . TYR   B 1 115 ? 14.481  30.547 67.477 1.000 21.874  ? 114 TYR   BBB CA  1 ? 
ATOM   2952 C  C   . TYR   B 1 115 ? 13.936  30.634 66.054 1.000 19.752  ? 114 TYR   BBB C   1 ? 
ATOM   2953 O  O   . TYR   B 1 115 ? 14.277  29.814 65.177 1.000 21.367  ? 114 TYR   BBB O   1 ? 
ATOM   2954 C  CB  . TYR   B 1 115 ? 15.324  31.759 67.936 1.000 20.569  ? 114 TYR   BBB CB  1 ? 
ATOM   2955 C  CG  . TYR   B 1 115 ? 15.428  31.872 69.433 1.000 22.798  ? 114 TYR   BBB CG  1 ? 
ATOM   2956 C  CD1 . TYR   B 1 115 ? 16.076  30.894 70.192 1.000 21.593  ? 114 TYR   BBB CD1 1 ? 
ATOM   2957 C  CD2 . TYR   B 1 115 ? 14.838  32.947 70.110 1.000 23.170  ? 114 TYR   BBB CD2 1 ? 
ATOM   2958 C  CE1 . TYR   B 1 115 ? 16.146  31.000 71.574 1.000 27.615  ? 114 TYR   BBB CE1 1 ? 
ATOM   2959 C  CE2 . TYR   B 1 115 ? 14.877  33.044 71.493 1.000 25.507  ? 114 TYR   BBB CE2 1 ? 
ATOM   2960 C  CZ  . TYR   B 1 115 ? 15.526  32.061 72.233 1.000 26.531  ? 114 TYR   BBB CZ  1 ? 
ATOM   2961 O  OH  . TYR   B 1 115 ? 15.558  32.158 73.599 1.000 30.600  ? 114 TYR   BBB OH  1 ? 
ATOM   2962 N  N   . SER   B 1 116 ? 13.172  31.693 65.767 1.000 20.454  ? 115 SER   BBB N   1 ? 
ATOM   2963 C  CA  A SER   B 1 116 ? 12.460  31.859 64.476 0.500 20.281  ? 115 SER   BBB CA  1 ? 
ATOM   2964 C  CA  B SER   B 1 116 ? 12.459  31.862 64.477 0.500 20.196  ? 115 SER   BBB CA  1 ? 
ATOM   2965 C  C   . SER   B 1 116 ? 13.399  32.410 63.391 1.000 20.023  ? 115 SER   BBB C   1 ? 
ATOM   2966 O  O   . SER   B 1 116 ? 13.082  32.223 62.194 1.000 22.771  ? 115 SER   BBB O   1 ? 
ATOM   2967 C  CB  A SER   B 1 116 ? 11.231  32.743 64.636 0.500 21.571  ? 115 SER   BBB CB  1 ? 
ATOM   2968 C  CB  B SER   B 1 116 ? 11.214  32.732 64.642 0.500 23.994  ? 115 SER   BBB CB  1 ? 
ATOM   2969 O  OG  A SER   B 1 116 ? 10.294  32.303 65.612 0.500 23.680  ? 115 SER   BBB OG  1 ? 
ATOM   2970 O  OG  B SER   B 1 116 ? 11.540  34.131 64.736 0.500 25.491  ? 115 SER   BBB OG  1 ? 
ATOM   2971 N  N   . ALA   B 1 117 ? 14.461  33.120 63.788 1.000 19.048  ? 116 ALA   BBB N   1 ? 
ATOM   2972 C  CA  . ALA   B 1 117 ? 15.380  33.722 62.808 1.000 18.125  ? 116 ALA   BBB CA  1 ? 
ATOM   2973 C  C   . ALA   B 1 117 ? 16.641  34.161 63.542 1.000 17.254  ? 116 ALA   BBB C   1 ? 
ATOM   2974 O  O   . ALA   B 1 117 ? 16.699  34.041 64.749 1.000 19.470  ? 116 ALA   BBB O   1 ? 
ATOM   2975 C  CB  . ALA   B 1 117 ? 14.723  34.912 62.119 1.000 17.698  ? 116 ALA   BBB CB  1 ? 
ATOM   2976 N  N   . GLU   B 1 118 ? 17.599  34.669 62.781 1.000 16.750  ? 117 GLU   BBB N   1 ? 
ATOM   2977 C  CA  . GLU   B 1 118 ? 18.888  35.098 63.350 1.000 16.405  ? 117 GLU   BBB CA  1 ? 
ATOM   2978 C  C   . GLU   B 1 118 ? 19.424  36.266 62.509 1.000 18.610  ? 117 GLU   BBB C   1 ? 
ATOM   2979 O  O   . GLU   B 1 118 ? 19.398  36.227 61.290 1.000 22.415  ? 117 GLU   BBB O   1 ? 
ATOM   2980 C  CB  . GLU   B 1 118 ? 19.868  33.924 63.417 1.000 19.635  ? 117 GLU   BBB CB  1 ? 
ATOM   2981 C  CG  . GLU   B 1 118 ? 21.106  34.213 64.252 1.000 18.738  ? 117 GLU   BBB CG  1 ? 
ATOM   2982 C  CD  . GLU   B 1 118 ? 21.895  32.967 64.619 1.000 18.306  ? 117 GLU   BBB CD  1 ? 
ATOM   2983 O  OE1 . GLU   B 1 118 ? 23.141  33.010 64.663 1.000 21.603  ? 117 GLU   BBB OE1 1 ? 
ATOM   2984 O  OE2 . GLU   B 1 118 ? 21.173  31.938 64.817 1.000 21.781  ? 117 GLU   BBB OE2 1 ? 
ATOM   2985 N  N   . LEU   B 1 119 ? 19.886  37.285 63.215 1.000 16.849  ? 118 LEU   BBB N   1 ? 
ATOM   2986 C  CA  . LEU   B 1 119 ? 20.623  38.393 62.567 1.000 17.934  ? 118 LEU   BBB CA  1 ? 
ATOM   2987 C  C   . LEU   B 1 119 ? 22.130  38.147 62.671 1.000 20.623  ? 118 LEU   BBB C   1 ? 
ATOM   2988 O  O   . LEU   B 1 119 ? 22.566  37.882 63.762 1.000 20.586  ? 118 LEU   BBB O   1 ? 
ATOM   2989 C  CB  . LEU   B 1 119 ? 20.227  39.687 63.295 1.000 17.954  ? 118 LEU   BBB CB  1 ? 
ATOM   2990 C  CG  . LEU   B 1 119 ? 21.104  40.940 63.051 1.000 18.528  ? 118 LEU   BBB CG  1 ? 
ATOM   2991 C  CD1 . LEU   B 1 119 ? 20.932  41.453 61.643 1.000 18.564  ? 118 LEU   BBB CD1 1 ? 
ATOM   2992 C  CD2 . LEU   B 1 119 ? 20.683  41.986 64.053 1.000 19.522  ? 118 LEU   BBB CD2 1 ? 
ATOM   2993 N  N   . HIS   B 1 120 ? 22.833  38.326 61.565 1.000 20.617  ? 119 HIS   BBB N   1 ? 
ATOM   2994 C  CA  . HIS   B 1 120 ? 24.339  38.335 61.550 1.000 19.857  ? 119 HIS   BBB CA  1 ? 
ATOM   2995 C  C   . HIS   B 1 120 ? 24.836  39.745 61.167 1.000 16.311  ? 119 HIS   BBB C   1 ? 
ATOM   2996 O  O   . HIS   B 1 120 ? 24.474  40.161 60.069 1.000 18.270  ? 119 HIS   BBB O   1 ? 
ATOM   2997 C  CB  . HIS   B 1 120 ? 24.890  37.254 60.598 1.000 16.849  ? 119 HIS   BBB CB  1 ? 
ATOM   2998 C  CG  . HIS   B 1 120 ? 24.585  35.869 61.101 1.000 17.942  ? 119 HIS   BBB CG  1 ? 
ATOM   2999 N  ND1 . HIS   B 1 120 ? 24.532  34.675 60.248 1.000 24.501  ? 119 HIS   BBB ND1 1 ? 
ATOM   3000 C  CD2 . HIS   B 1 120 ? 24.304  35.509 62.384 1.000 16.435  ? 119 HIS   BBB CD2 1 ? 
ATOM   3001 C  CE1 . HIS   B 1 120 ? 24.267  33.671 61.071 1.000 16.895  ? 119 HIS   BBB CE1 1 ? 
ATOM   3002 N  NE2 . HIS   B 1 120 ? 24.122  34.089 62.370 1.000 16.801  ? 119 HIS   BBB NE2 1 ? 
ATOM   3003 N  N   . VAL   B 1 121 ? 25.755  40.279 61.966 1.000 18.485  ? 120 VAL   BBB N   1 ? 
ATOM   3004 C  CA  . VAL   B 1 121 ? 26.466  41.571 61.681 1.000 17.931  ? 120 VAL   BBB CA  1 ? 
ATOM   3005 C  C   . VAL   B 1 121 ? 27.961  41.189 61.571 1.000 19.821  ? 120 VAL   BBB C   1 ? 
ATOM   3006 O  O   . VAL   B 1 121 ? 28.544  40.862 62.590 1.000 21.736  ? 120 VAL   BBB O   1 ? 
ATOM   3007 C  CB  . VAL   B 1 121 ? 26.186  42.607 62.775 1.000 20.067  ? 120 VAL   BBB CB  1 ? 
ATOM   3008 C  CG1 . VAL   B 1 121 ? 26.774  43.980 62.377 1.000 22.987  ? 120 VAL   BBB CG1 1 ? 
ATOM   3009 C  CG2 . VAL   B 1 121 ? 24.695  42.719 63.050 1.000 23.333  ? 120 VAL   BBB CG2 1 ? 
ATOM   3010 N  N   . ALA   B 1 122 ? 28.486  41.203 60.325 1.000 19.269  ? 121 ALA   BBB N   1 ? 
ATOM   3011 C  CA  . ALA   B 1 122 ? 29.813  40.683 59.946 1.000 18.778  ? 121 ALA   BBB CA  1 ? 
ATOM   3012 C  C   . ALA   B 1 122 ? 30.848  41.803 59.852 1.000 19.416  ? 121 ALA   BBB C   1 ? 
ATOM   3013 O  O   . ALA   B 1 122 ? 30.482  42.895 59.338 1.000 23.303  ? 121 ALA   BBB O   1 ? 
ATOM   3014 C  CB  . ALA   B 1 122 ? 29.702  39.918 58.642 1.000 19.219  ? 121 ALA   BBB CB  1 ? 
ATOM   3015 N  N   . HIS   B 1 123 ? 32.058  41.526 60.289 1.000 19.245  ? 122 HIS   BBB N   1 ? 
ATOM   3016 C  CA  . HIS   B 1 123 ? 33.188  42.470 60.379 1.000 20.082  ? 122 HIS   BBB CA  1 ? 
ATOM   3017 C  C   . HIS   B 1 123 ? 34.479  41.765 59.985 1.000 22.273  ? 122 HIS   BBB C   1 ? 
ATOM   3018 O  O   . HIS   B 1 123 ? 34.550  40.535 60.191 1.000 22.668  ? 122 HIS   BBB O   1 ? 
ATOM   3019 C  CB  . HIS   B 1 123 ? 33.345  42.992 61.808 1.000 19.099  ? 122 HIS   BBB CB  1 ? 
ATOM   3020 C  CG  . HIS   B 1 123 ? 32.101  43.401 62.490 1.000 19.106  ? 122 HIS   BBB CG  1 ? 
ATOM   3021 N  ND1 . HIS   B 1 123 ? 31.141  42.520 62.917 1.000 22.123  ? 122 HIS   BBB ND1 1 ? 
ATOM   3022 C  CD2 . HIS   B 1 123 ? 31.673  44.643 62.835 1.000 23.212  ? 122 HIS   BBB CD2 1 ? 
ATOM   3023 C  CE1 . HIS   B 1 123 ? 30.163  43.165 63.529 1.000 21.503  ? 122 HIS   BBB CE1 1 ? 
ATOM   3024 N  NE2 . HIS   B 1 123 ? 30.498  44.538 63.490 1.000 20.204  ? 122 HIS   BBB NE2 1 ? 
ATOM   3025 N  N   . TRP   B 1 124 ? 35.476  42.484 59.473 1.000 24.698  ? 123 TRP   BBB N   1 ? 
ATOM   3026 C  CA  . TRP   B 1 124 ? 36.806  41.901 59.153 1.000 24.617  ? 123 TRP   BBB CA  1 ? 
ATOM   3027 C  C   . TRP   B 1 124 ? 37.941  42.640 59.885 1.000 22.860  ? 123 TRP   BBB C   1 ? 
ATOM   3028 O  O   . TRP   B 1 124 ? 37.815  43.813 60.204 1.000 27.101  ? 123 TRP   BBB O   1 ? 
ATOM   3029 C  CB  . TRP   B 1 124 ? 37.030  41.765 57.633 1.000 24.555  ? 123 TRP   BBB CB  1 ? 
ATOM   3030 C  CG  . TRP   B 1 124 ? 37.132  43.039 56.856 1.000 28.138  ? 123 TRP   BBB CG  1 ? 
ATOM   3031 C  CD1 . TRP   B 1 124 ? 36.115  43.720 56.247 1.000 26.072  ? 123 TRP   BBB CD1 1 ? 
ATOM   3032 C  CD2 . TRP   B 1 124 ? 38.332  43.711 56.461 1.000 34.173  ? 123 TRP   BBB CD2 1 ? 
ATOM   3033 N  NE1 . TRP   B 1 124 ? 36.586  44.815 55.567 1.000 31.665  ? 123 TRP   BBB NE1 1 ? 
ATOM   3034 C  CE2 . TRP   B 1 124 ? 37.946  44.828 55.677 1.000 36.439  ? 123 TRP   BBB CE2 1 ? 
ATOM   3035 C  CE3 . TRP   B 1 124 ? 39.684  43.501 56.728 1.000 35.186  ? 123 TRP   BBB CE3 1 ? 
ATOM   3036 C  CZ2 . TRP   B 1 124 ? 38.865  45.748 55.186 1.000 41.261  ? 123 TRP   BBB CZ2 1 ? 
ATOM   3037 C  CZ3 . TRP   B 1 124 ? 40.594  44.402 56.223 1.000 44.617  ? 123 TRP   BBB CZ3 1 ? 
ATOM   3038 C  CH2 . TRP   B 1 124 ? 40.183  45.497 55.461 1.000 47.976  ? 123 TRP   BBB CH2 1 ? 
ATOM   3039 N  N   . ASN   B 1 125 ? 39.057  41.952 60.114 1.000 27.387  ? 124 ASN   BBB N   1 ? 
ATOM   3040 C  CA  . ASN   B 1 125 ? 40.182  42.466 60.938 1.000 27.974  ? 124 ASN   BBB CA  1 ? 
ATOM   3041 C  C   . ASN   B 1 125 ? 41.040  43.432 60.100 1.000 29.637  ? 124 ASN   BBB C   1 ? 
ATOM   3042 O  O   . ASN   B 1 125 ? 42.007  42.943 59.453 1.000 30.660  ? 124 ASN   BBB O   1 ? 
ATOM   3043 C  CB  . ASN   B 1 125 ? 41.004  41.291 61.470 1.000 29.494  ? 124 ASN   BBB CB  1 ? 
ATOM   3044 C  CG  . ASN   B 1 125 ? 41.991  41.695 62.532 1.000 31.962  ? 124 ASN   BBB CG  1 ? 
ATOM   3045 O  OD1 . ASN   B 1 125 ? 42.400  40.864 63.338 1.000 39.773  ? 124 ASN   BBB OD1 1 ? 
ATOM   3046 N  ND2 . ASN   B 1 125 ? 42.371  42.959 62.547 1.000 35.549  ? 124 ASN   BBB ND2 1 ? 
ATOM   3047 N  N   . SER   B 1 126 ? 40.712  44.727 60.101 1.000 35.850  ? 125 SER   BBB N   1 ? 
ATOM   3048 C  CA  . SER   B 1 126 ? 41.532  45.758 59.379 1.000 42.061  ? 125 SER   BBB CA  1 ? 
ATOM   3049 C  C   . SER   B 1 126 ? 42.804  46.137 60.145 1.000 46.924  ? 125 SER   BBB C   1 ? 
ATOM   3050 O  O   . SER   B 1 126 ? 43.600  46.890 59.565 1.000 50.989  ? 125 SER   BBB O   1 ? 
ATOM   3051 C  CB  . SER   B 1 126 ? 40.746  46.995 59.056 1.000 49.957  ? 125 SER   BBB CB  1 ? 
ATOM   3052 O  OG  . SER   B 1 126 ? 40.076  47.422 60.227 1.000 42.257  ? 125 SER   BBB OG  1 ? 
ATOM   3053 N  N   . ALA   B 1 127 ? 42.953  45.747 61.408 1.000 45.157  ? 126 ALA   BBB N   1 ? 
ATOM   3054 C  CA  . ALA   B 1 127 ? 44.175  46.081 62.176 1.000 42.527  ? 126 ALA   BBB CA  1 ? 
ATOM   3055 C  C   . ALA   B 1 127 ? 45.330  45.266 61.592 1.000 40.793  ? 126 ALA   BBB C   1 ? 
ATOM   3056 O  O   . ALA   B 1 127 ? 46.397  45.819 61.399 1.000 44.718  ? 126 ALA   BBB O   1 ? 
ATOM   3057 C  CB  . ALA   B 1 127 ? 43.976  45.836 63.652 1.000 40.829  ? 126 ALA   BBB CB  1 ? 
ATOM   3058 N  N   . LYS   B 1 128 ? 45.073  44.011 61.232 1.000 34.829  ? 127 LYS   BBB N   1 ? 
ATOM   3059 C  CA  . LYS   B 1 128 ? 46.119  43.035 60.839 1.000 41.000  ? 127 LYS   BBB CA  1 ? 
ATOM   3060 C  C   . LYS   B 1 128 ? 46.178  42.889 59.319 1.000 42.895  ? 127 LYS   BBB C   1 ? 
ATOM   3061 O  O   . LYS   B 1 128 ? 47.269  42.573 58.810 1.000 42.070  ? 127 LYS   BBB O   1 ? 
ATOM   3062 C  CB  . LYS   B 1 128 ? 45.796  41.660 61.424 1.000 43.147  ? 127 LYS   BBB CB  1 ? 
ATOM   3063 C  CG  . LYS   B 1 128 ? 45.862  41.578 62.945 1.000 51.180  ? 127 LYS   BBB CG  1 ? 
ATOM   3064 C  CD  . LYS   B 1 128 ? 46.783  40.501 63.459 1.000 64.625  ? 127 LYS   BBB CD  1 ? 
ATOM   3065 C  CE  . LYS   B 1 128 ? 46.760  39.238 62.622 1.000 66.563  ? 127 LYS   BBB CE  1 ? 
ATOM   3066 N  NZ  . LYS   B 1 128 ? 47.509  38.138 63.277 1.000 75.429  ? 127 LYS   BBB NZ  1 ? 
ATOM   3067 N  N   . TYR   B 1 129 ? 45.029  43.015 58.647 1.000 37.257  ? 128 TYR   BBB N   1 ? 
ATOM   3068 C  CA  . TYR   B 1 129 ? 44.893  42.712 57.200 1.000 31.445  ? 128 TYR   BBB CA  1 ? 
ATOM   3069 C  C   . TYR   B 1 129 ? 44.447  43.979 56.458 1.000 34.236  ? 128 TYR   BBB C   1 ? 
ATOM   3070 O  O   . TYR   B 1 129 ? 43.918  44.925 57.118 1.000 37.926  ? 128 TYR   BBB O   1 ? 
ATOM   3071 C  CB  . TYR   B 1 129 ? 43.972  41.508 57.011 1.000 33.760  ? 128 TYR   BBB CB  1 ? 
ATOM   3072 C  CG  . TYR   B 1 129 ? 44.356  40.372 57.919 1.000 38.947  ? 128 TYR   BBB CG  1 ? 
ATOM   3073 C  CD1 . TYR   B 1 129 ? 45.623  39.817 57.828 1.000 40.878  ? 128 TYR   BBB CD1 1 ? 
ATOM   3074 C  CD2 . TYR   B 1 129 ? 43.493  39.878 58.888 1.000 35.632  ? 128 TYR   BBB CD2 1 ? 
ATOM   3075 C  CE1 . TYR   B 1 129 ? 46.028  38.789 58.664 1.000 47.281  ? 128 TYR   BBB CE1 1 ? 
ATOM   3076 C  CE2 . TYR   B 1 129 ? 43.897  38.864 59.745 1.000 43.153  ? 128 TYR   BBB CE2 1 ? 
ATOM   3077 C  CZ  . TYR   B 1 129 ? 45.163  38.313 59.629 1.000 43.353  ? 128 TYR   BBB CZ  1 ? 
ATOM   3078 O  OH  . TYR   B 1 129 ? 45.567  37.276 60.432 1.000 44.219  ? 128 TYR   BBB OH  1 ? 
ATOM   3079 N  N   . SER   B 1 130 ? 44.690  44.030 55.146 1.000 43.079  ? 129 SER   BBB N   1 ? 
ATOM   3080 C  CA  . SER   B 1 130 ? 44.364  45.238 54.332 1.000 42.541  ? 129 SER   BBB CA  1 ? 
ATOM   3081 C  C   . SER   B 1 130 ? 43.106  45.021 53.501 1.000 48.779  ? 129 SER   BBB C   1 ? 
ATOM   3082 O  O   . SER   B 1 130 ? 42.597  46.027 52.990 1.000 58.536  ? 129 SER   BBB O   1 ? 
ATOM   3083 C  CB  . SER   B 1 130 ? 45.486  45.677 53.434 1.000 34.387  ? 129 SER   BBB CB  1 ? 
ATOM   3084 O  OG  . SER   B 1 130 ? 46.693  45.800 54.169 1.000 32.990  ? 129 SER   BBB OG  1 ? 
ATOM   3085 N  N   . SER   B 1 131 ? 42.600  43.781 53.370 1.000 42.541  ? 130 SER   BBB N   1 ? 
ATOM   3086 C  CA  . SER   B 1 131 ? 41.342  43.550 52.612 1.000 45.300  ? 130 SER   BBB CA  1 ? 
ATOM   3087 C  C   . SER   B 1 131 ? 40.546  42.375 53.178 1.000 51.166  ? 130 SER   BBB C   1 ? 
ATOM   3088 O  O   . SER   B 1 131 ? 41.140  41.474 53.785 1.000 41.978  ? 130 SER   BBB O   1 ? 
ATOM   3089 C  CB  . SER   B 1 131 ? 41.658  43.370 51.173 1.000 42.411  ? 130 SER   BBB CB  1 ? 
ATOM   3090 O  OG  . SER   B 1 131 ? 42.190  42.078 50.957 1.000 45.085  ? 130 SER   BBB OG  1 ? 
ATOM   3091 N  N   . LEU   B 1 132 ? 39.252  42.433 52.917 1.000 52.760  ? 131 LEU   BBB N   1 ? 
ATOM   3092 C  CA  . LEU   B 1 132 ? 38.333  41.323 53.209 1.000 37.394  ? 131 LEU   BBB CA  1 ? 
ATOM   3093 C  C   . LEU   B 1 132 ? 38.920  40.019 52.641 1.000 38.865  ? 131 LEU   BBB C   1 ? 
ATOM   3094 O  O   . LEU   B 1 132 ? 38.931  39.041 53.402 1.000 33.901  ? 131 LEU   BBB O   1 ? 
ATOM   3095 C  CB  . LEU   B 1 132 ? 36.924  41.645 52.684 1.000 36.332  ? 131 LEU   BBB CB  1 ? 
ATOM   3096 C  CG  . LEU   B 1 132 ? 35.898  40.534 52.932 1.000 34.799  ? 131 LEU   BBB CG  1 ? 
ATOM   3097 C  CD1 . LEU   B 1 132 ? 35.728  40.233 54.419 1.000 27.161  ? 131 LEU   BBB CD1 1 ? 
ATOM   3098 C  CD2 . LEU   B 1 132 ? 34.539  40.857 52.306 1.000 37.585  ? 131 LEU   BBB CD2 1 ? 
ATOM   3099 N  N   . ALA   B 1 133 ? 39.444  39.987 51.403 1.000 33.081  ? 132 ALA   BBB N   1 ? 
ATOM   3100 C  CA  . ALA   B 1 133 ? 39.974  38.735 50.803 1.000 38.633  ? 132 ALA   BBB CA  1 ? 
ATOM   3101 C  C   . ALA   B 1 133 ? 41.142  38.204 51.647 1.000 38.045  ? 132 ALA   BBB C   1 ? 
ATOM   3102 O  O   . ALA   B 1 133 ? 41.227  36.978 51.833 1.000 43.443  ? 132 ALA   BBB O   1 ? 
ATOM   3103 C  CB  . ALA   B 1 133 ? 40.382  38.976 49.371 1.000 51.499  ? 132 ALA   BBB CB  1 ? 
ATOM   3104 N  N   . GLU   B 1 134 ? 42.025  39.092 52.120 1.000 41.747  ? 133 GLU   BBB N   1 ? 
ATOM   3105 C  CA  . GLU   B 1 134 ? 43.201  38.711 52.956 1.000 40.849  ? 133 GLU   BBB CA  1 ? 
ATOM   3106 C  C   . GLU   B 1 134 ? 42.706  38.190 54.311 1.000 37.909  ? 133 GLU   BBB C   1 ? 
ATOM   3107 O  O   . GLU   B 1 134 ? 43.339  37.262 54.833 1.000 39.657  ? 133 GLU   BBB O   1 ? 
ATOM   3108 C  CB  . GLU   B 1 134 ? 44.173  39.885 53.135 1.000 38.884  ? 133 GLU   BBB CB  1 ? 
ATOM   3109 C  CG  . GLU   B 1 134 ? 45.528  39.494 53.712 1.000 32.429  ? 133 GLU   BBB CG  1 ? 
ATOM   3110 C  CD  . GLU   B 1 134 ? 46.392  40.686 54.106 1.000 39.752  ? 133 GLU   BBB CD  1 ? 
ATOM   3111 O  OE1 . GLU   B 1 134 ? 47.461  40.480 54.740 1.000 45.853  ? 133 GLU   BBB OE1 1 ? 
ATOM   3112 O  OE2 . GLU   B 1 134 ? 45.988  41.827 53.786 1.000 45.906  ? 133 GLU   BBB OE2 1 ? 
ATOM   3113 N  N   . ALA   B 1 135 ? 41.644  38.777 54.866 1.000 38.096  ? 134 ALA   BBB N   1 ? 
ATOM   3114 C  CA  . ALA   B 1 135 ? 41.153  38.500 56.238 1.000 36.836  ? 134 ALA   BBB CA  1 ? 
ATOM   3115 C  C   . ALA   B 1 135 ? 40.286  37.236 56.251 1.000 35.509  ? 134 ALA   BBB C   1 ? 
ATOM   3116 O  O   . ALA   B 1 135 ? 40.311  36.525 57.264 1.000 37.344  ? 134 ALA   BBB O   1 ? 
ATOM   3117 C  CB  . ALA   B 1 135 ? 40.384  39.686 56.766 1.000 37.734  ? 134 ALA   BBB CB  1 ? 
ATOM   3118 N  N   . ALA   B 1 136 ? 39.580  36.944 55.164 1.000 35.983  ? 135 ALA   BBB N   1 ? 
ATOM   3119 C  CA  . ALA   B 1 136 ? 38.438  36.000 55.161 1.000 34.257  ? 135 ALA   BBB CA  1 ? 
ATOM   3120 C  C   . ALA   B 1 136 ? 38.852  34.542 55.415 1.000 35.241  ? 135 ALA   BBB C   1 ? 
ATOM   3121 O  O   . ALA   B 1 136 ? 37.962  33.793 55.852 1.000 35.655  ? 135 ALA   BBB O   1 ? 
ATOM   3122 C  CB  . ALA   B 1 136 ? 37.652  36.136 53.885 1.000 37.485  ? 135 ALA   BBB CB  1 ? 
ATOM   3123 N  N   . SER   B 1 137 ? 40.096  34.115 55.172 1.000 30.391  ? 136 SER   BBB N   1 ? 
ATOM   3124 C  CA  . SER   B 1 137 ? 40.515  32.704 55.454 1.000 35.304  ? 136 SER   BBB CA  1 ? 
ATOM   3125 C  C   . SER   B 1 137 ? 41.492  32.640 56.638 1.000 35.715  ? 136 SER   BBB C   1 ? 
ATOM   3126 O  O   . SER   B 1 137 ? 42.070  31.548 56.882 1.000 45.253  ? 136 SER   BBB O   1 ? 
ATOM   3127 C  CB  . SER   B 1 137 ? 41.071  32.022 54.218 1.000 33.324  ? 136 SER   BBB CB  1 ? 
ATOM   3128 O  OG  . SER   B 1 137 ? 42.247  32.667 53.743 1.000 43.745  ? 136 SER   BBB OG  1 ? 
ATOM   3129 N  N   . LYS   B 1 138 ? 41.651  33.743 57.370 1.000 34.466  ? 137 LYS   BBB N   1 ? 
ATOM   3130 C  CA  . LYS   B 1 138 ? 42.533  33.819 58.564 1.000 36.060  ? 137 LYS   BBB CA  1 ? 
ATOM   3131 C  C   . LYS   B 1 138 ? 41.724  33.422 59.797 1.000 29.672  ? 137 LYS   BBB C   1 ? 
ATOM   3132 O  O   . LYS   B 1 138 ? 40.571  33.825 59.891 1.000 28.454  ? 137 LYS   BBB O   1 ? 
ATOM   3133 C  CB  . LYS   B 1 138 ? 43.094  35.230 58.752 1.000 36.798  ? 137 LYS   BBB CB  1 ? 
ATOM   3134 C  CG  . LYS   B 1 138 ? 43.931  35.746 57.592 1.000 41.953  ? 137 LYS   BBB CG  1 ? 
ATOM   3135 C  CD  . LYS   B 1 138 ? 45.266  35.042 57.472 1.000 45.338  ? 137 LYS   BBB CD  1 ? 
ATOM   3136 C  CE  . LYS   B 1 138 ? 46.148  35.601 56.380 1.000 47.233  ? 137 LYS   BBB CE  1 ? 
ATOM   3137 N  NZ  . LYS   B 1 138 ? 45.600  35.278 55.041 1.000 46.850  ? 137 LYS   BBB NZ  1 ? 
ATOM   3138 N  N   . ALA   B 1 139 ? 42.316  32.676 60.725 1.000 33.898  ? 138 ALA   BBB N   1 ? 
ATOM   3139 C  CA  . ALA   B 1 139 ? 41.616  32.202 61.948 1.000 32.155  ? 138 ALA   BBB CA  1 ? 
ATOM   3140 C  C   . ALA   B 1 139 ? 41.057  33.425 62.695 1.000 25.715  ? 138 ALA   BBB C   1 ? 
ATOM   3141 O  O   . ALA   B 1 139 ? 39.944  33.359 63.219 1.000 31.274  ? 138 ALA   BBB O   1 ? 
ATOM   3142 C  CB  . ALA   B 1 139 ? 42.536  31.373 62.820 1.000 31.259  ? 138 ALA   BBB CB  1 ? 
ATOM   3143 N  N   . ASP   B 1 140 ? 41.799  34.537 62.662 1.000 30.651  ? 139 ASP   BBB N   1 ? 
ATOM   3144 C  CA  . ASP   B 1 140 ? 41.481  35.779 63.404 1.000 27.380  ? 139 ASP   BBB CA  1 ? 
ATOM   3145 C  C   . ASP   B 1 140 ? 40.878  36.845 62.456 1.000 28.839  ? 139 ASP   BBB C   1 ? 
ATOM   3146 O  O   . ASP   B 1 140 ? 40.897  38.049 62.813 1.000 32.939  ? 139 ASP   BBB O   1 ? 
ATOM   3147 C  CB  . ASP   B 1 140 ? 42.744  36.227 64.140 1.000 28.878  ? 139 ASP   BBB CB  1 ? 
ATOM   3148 C  CG  . ASP   B 1 140 ? 43.879  36.667 63.230 1.000 32.035  ? 139 ASP   BBB CG  1 ? 
ATOM   3149 O  OD1 . ASP   B 1 140 ? 43.748  36.536 62.014 1.000 36.913  ? 139 ASP   BBB OD1 1 ? 
ATOM   3150 O  OD2 . ASP   B 1 140 ? 44.913  37.073 63.755 1.000 38.143  ? 139 ASP   BBB OD2 1 ? 
ATOM   3151 N  N   . GLY   B 1 141 ? 40.408  36.452 61.269 1.000 30.125  ? 140 GLY   BBB N   1 ? 
ATOM   3152 C  CA  . GLY   B 1 141 ? 40.076  37.405 60.191 1.000 25.798  ? 140 GLY   BBB CA  1 ? 
ATOM   3153 C  C   . GLY   B 1 141 ? 38.718  38.074 60.342 1.000 26.254  ? 140 GLY   BBB C   1 ? 
ATOM   3154 O  O   . GLY   B 1 141 ? 38.600  39.306 60.008 1.000 31.276  ? 140 GLY   BBB O   1 ? 
ATOM   3155 N  N   . LEU   B 1 142 ? 37.710  37.309 60.757 1.000 25.198  ? 141 LEU   BBB N   1 ? 
ATOM   3156 C  CA  . LEU   B 1 142 ? 36.298  37.755 60.805 1.000 21.870  ? 141 LEU   BBB CA  1 ? 
ATOM   3157 C  C   . LEU   B 1 142 ? 35.718  37.683 62.216 1.000 24.933  ? 141 LEU   BBB C   1 ? 
ATOM   3158 O  O   . LEU   B 1 142 ? 36.085  36.796 63.035 1.000 22.463  ? 141 LEU   BBB O   1 ? 
ATOM   3159 C  CB  . LEU   B 1 142 ? 35.435  36.938 59.846 1.000 22.716  ? 141 LEU   BBB CB  1 ? 
ATOM   3160 C  CG  . LEU   B 1 142 ? 35.945  36.813 58.415 1.000 24.000  ? 141 LEU   BBB CG  1 ? 
ATOM   3161 C  CD1 . LEU   B 1 142 ? 34.993  35.965 57.572 1.000 26.391  ? 141 LEU   BBB CD1 1 ? 
ATOM   3162 C  CD2 . LEU   B 1 142 ? 36.130  38.162 57.785 1.000 25.262  ? 141 LEU   BBB CD2 1 ? 
ATOM   3163 N  N   . ALA   B 1 143 ? 34.768  38.584 62.445 1.000 21.349  ? 142 ALA   BBB N   1 ? 
ATOM   3164 C  CA  . ALA   B 1 143 ? 33.961  38.673 63.670 1.000 21.209  ? 142 ALA   BBB CA  1 ? 
ATOM   3165 C  C   . ALA   B 1 143 ? 32.493  38.860 63.284 1.000 21.417  ? 142 ALA   BBB C   1 ? 
ATOM   3166 O  O   . ALA   B 1 143 ? 32.161  39.790 62.531 1.000 19.641  ? 142 ALA   BBB O   1 ? 
ATOM   3167 C  CB  . ALA   B 1 143 ? 34.436  39.778 64.579 1.000 24.199  ? 142 ALA   BBB CB  1 ? 
ATOM   3168 N  N   . VAL   B 1 144 ? 31.626  37.970 63.750 1.000 19.979  ? 143 VAL   BBB N   1 ? 
ATOM   3169 C  CA  . VAL   B 1 144 ? 30.192  38.069 63.423 1.000 17.462  ? 143 VAL   BBB CA  1 ? 
ATOM   3170 C  C   . VAL   B 1 144 ? 29.415  38.086 64.731 1.000 18.064  ? 143 VAL   BBB C   1 ? 
ATOM   3171 O  O   . VAL   B 1 144 ? 29.654  37.259 65.627 1.000 19.358  ? 143 VAL   BBB O   1 ? 
ATOM   3172 C  CB  . VAL   B 1 144 ? 29.688  36.969 62.468 1.000 19.220  ? 143 VAL   BBB CB  1 ? 
ATOM   3173 C  CG1 . VAL   B 1 144 ? 28.274  37.238 62.048 1.000 24.313  ? 143 VAL   BBB CG1 1 ? 
ATOM   3174 C  CG2 . VAL   B 1 144 ? 30.580  36.804 61.244 1.000 21.348  ? 143 VAL   BBB CG2 1 ? 
ATOM   3175 N  N   . ILE   B 1 145 ? 28.564  39.104 64.883 1.000 20.870  ? 144 ILE   BBB N   1 ? 
ATOM   3176 C  CA  . ILE   B 1 145 ? 27.587  39.173 65.989 1.000 20.149  ? 144 ILE   BBB CA  1 ? 
ATOM   3177 C  C   . ILE   B 1 145 ? 26.311  38.494 65.526 1.000 18.268  ? 144 ILE   BBB C   1 ? 
ATOM   3178 O  O   . ILE   B 1 145 ? 25.822  38.807 64.442 1.000 21.887  ? 144 ILE   BBB O   1 ? 
ATOM   3179 C  CB  . ILE   B 1 145 ? 27.274  40.642 66.368 1.000 21.429  ? 144 ILE   BBB CB  1 ? 
ATOM   3180 C  CG1 . ILE   B 1 145 ? 28.552  41.300 66.854 1.000 21.718  ? 144 ILE   BBB CG1 1 ? 
ATOM   3181 C  CG2 . ILE   B 1 145 ? 26.186  40.666 67.415 1.000 21.750  ? 144 ILE   BBB CG2 1 ? 
ATOM   3182 C  CD1 . ILE   B 1 145 ? 28.382  42.836 66.921 1.000 23.236  ? 144 ILE   BBB CD1 1 ? 
ATOM   3183 N  N   . GLY   B 1 146 ? 25.900  37.447 66.266 1.000 20.740  ? 145 GLY   BBB N   1 ? 
ATOM   3184 C  CA  . GLY   B 1 146 ? 24.560  36.906 66.088 1.000 19.698  ? 145 GLY   BBB CA  1 ? 
ATOM   3185 C  C   . GLY   B 1 146 ? 23.587  37.250 67.171 1.000 21.991  ? 145 GLY   BBB C   1 ? 
ATOM   3186 O  O   . GLY   B 1 146 ? 23.903  37.190 68.351 1.000 21.818  ? 145 GLY   BBB O   1 ? 
ATOM   3187 N  N   . VAL   B 1 147 ? 22.379  37.548 66.710 1.000 18.466  ? 146 VAL   BBB N   1 ? 
ATOM   3188 C  CA  . VAL   B 1 147 ? 21.209  37.844 67.565 1.000 18.186  ? 146 VAL   BBB CA  1 ? 
ATOM   3189 C  C   . VAL   B 1 147 ? 20.052  36.928 67.179 1.000 15.164  ? 146 VAL   BBB C   1 ? 
ATOM   3190 O  O   . VAL   B 1 147 ? 19.614  36.944 66.023 1.000 16.707  ? 146 VAL   BBB O   1 ? 
ATOM   3191 C  CB  . VAL   B 1 147 ? 20.759  39.305 67.402 1.000 18.393  ? 146 VAL   BBB CB  1 ? 
ATOM   3192 C  CG1 . VAL   B 1 147 ? 19.643  39.595 68.360 1.000 20.310  ? 146 VAL   BBB CG1 1 ? 
ATOM   3193 C  CG2 . VAL   B 1 147 ? 21.963  40.236 67.593 1.000 17.612  ? 146 VAL   BBB CG2 1 ? 
ATOM   3194 N  N   . LEU   B 1 148 ? 19.591  36.193 68.173 1.000 15.756  ? 147 LEU   BBB N   1 ? 
ATOM   3195 C  CA  . LEU   B 1 148 ? 18.407  35.326 68.022 1.000 15.966  ? 147 LEU   BBB CA  1 ? 
ATOM   3196 C  C   . LEU   B 1 148 ? 17.141  36.175 67.944 1.000 16.215  ? 147 LEU   BBB C   1 ? 
ATOM   3197 O  O   . LEU   B 1 148 ? 17.028  37.161 68.712 1.000 18.651  ? 147 LEU   BBB O   1 ? 
ATOM   3198 C  CB  . LEU   B 1 148 ? 18.396  34.310 69.177 1.000 19.065  ? 147 LEU   BBB CB  1 ? 
ATOM   3199 C  CG  . LEU   B 1 148 ? 19.632  33.412 69.213 1.000 21.058  ? 147 LEU   BBB CG  1 ? 
ATOM   3200 C  CD1 . LEU   B 1 148 ? 19.748  32.696 70.544 1.000 25.382  ? 147 LEU   BBB CD1 1 ? 
ATOM   3201 C  CD2 . LEU   B 1 148 ? 19.643  32.431 68.044 1.000 24.015  ? 147 LEU   BBB CD2 1 ? 
ATOM   3202 N  N   . MET   B 1 149 ? 16.245  35.807 67.044 1.000 18.837  ? 148 MET   BBB N   1 ? 
ATOM   3203 C  CA  . MET   B 1 149 ? 14.973  36.492 66.757 1.000 20.383  ? 148 MET   BBB CA  1 ? 
ATOM   3204 C  C   . MET   B 1 149 ? 13.813  35.607 67.163 1.000 17.857  ? 148 MET   BBB C   1 ? 
ATOM   3205 O  O   . MET   B 1 149 ? 13.792  34.413 66.684 1.000 20.769  ? 148 MET   BBB O   1 ? 
ATOM   3206 C  CB  . MET   B 1 149 ? 14.945  36.845 65.273 1.000 20.489  ? 148 MET   BBB CB  1 ? 
ATOM   3207 C  CG  . MET   B 1 149 ? 16.060  37.901 64.975 1.000 19.732  ? 148 MET   BBB CG  1 ? 
ATOM   3208 S  SD  . MET   B 1 149 ? 16.241  38.259 63.252 1.000 19.682  ? 148 MET   BBB SD  1 ? 
ATOM   3209 C  CE  . MET   B 1 149 ? 14.787  39.294 63.046 1.000 22.251  ? 148 MET   BBB CE  1 ? 
ATOM   3210 N  N   . LYS   B 1 150 ? 13.043  36.043 68.131 1.000 17.103  ? 149 LYS   BBB N   1 ? 
ATOM   3211 C  CA  . LYS   B 1 150 ? 11.921  35.287 68.709 1.000 18.407  ? 149 LYS   BBB CA  1 ? 
ATOM   3212 C  C   . LYS   B 1 150 ? 10.597  35.783 68.140 1.000 19.305  ? 149 LYS   BBB C   1 ? 
ATOM   3213 O  O   . LYS   B 1 150 ? 10.281  36.991 68.257 1.000 20.127  ? 149 LYS   BBB O   1 ? 
ATOM   3214 C  CB  . LYS   B 1 150 ? 11.939  35.437 70.221 1.000 22.573  ? 149 LYS   BBB CB  1 ? 
ATOM   3215 C  CG  . LYS   B 1 150 ? 10.841  34.675 70.938 1.000 26.002  ? 149 LYS   BBB CG  1 ? 
ATOM   3216 C  CD  . LYS   B 1 150 ? 10.909  34.812 72.429 1.000 34.218  ? 149 LYS   BBB CD  1 ? 
ATOM   3217 C  CE  . LYS   B 1 150 ? 9.835   33.970 73.080 1.000 44.081  ? 149 LYS   BBB CE  1 ? 
ATOM   3218 N  NZ  . LYS   B 1 150 ? 9.806   34.198 74.536 1.000 60.449  ? 149 LYS   BBB NZ  1 ? 
ATOM   3219 N  N   . VAL   B 1 151 ? 9.820   34.901 67.539 1.000 19.762  ? 150 VAL   BBB N   1 ? 
ATOM   3220 C  CA  . VAL   B 1 151 ? 8.525   35.280 66.936 1.000 20.444  ? 150 VAL   BBB CA  1 ? 
ATOM   3221 C  C   . VAL   B 1 151 ? 7.604   35.809 68.046 1.000 20.668  ? 150 VAL   BBB C   1 ? 
ATOM   3222 O  O   . VAL   B 1 151 ? 7.545   35.246 69.157 1.000 22.516  ? 150 VAL   BBB O   1 ? 
ATOM   3223 C  CB  . VAL   B 1 151 ? 7.882   34.166 66.095 1.000 24.730  ? 150 VAL   BBB CB  1 ? 
ATOM   3224 C  CG1 . VAL   B 1 151 ? 7.442   32.980 66.961 1.000 24.182  ? 150 VAL   BBB CG1 1 ? 
ATOM   3225 C  CG2 . VAL   B 1 151 ? 6.731   34.736 65.272 1.000 26.846  ? 150 VAL   BBB CG2 1 ? 
ATOM   3226 N  N   . GLY   B 1 152 ? 7.014   36.993 67.786 1.000 19.249  ? 151 GLY   BBB N   1 ? 
ATOM   3227 C  CA  . GLY   B 1 152 ? 6.100   37.674 68.707 1.000 23.898  ? 151 GLY   BBB CA  1 ? 
ATOM   3228 C  C   . GLY   B 1 152 ? 5.634   38.965 68.088 1.000 23.371  ? 151 GLY   BBB C   1 ? 
ATOM   3229 O  O   . GLY   B 1 152 ? 5.132   38.935 66.956 1.000 23.991  ? 151 GLY   BBB O   1 ? 
ATOM   3230 N  N   . GLU   B 1 153 ? 5.787   40.064 68.818 1.000 24.670  ? 152 GLU   BBB N   1 ? 
ATOM   3231 C  CA  . GLU   B 1 153 ? 5.412   41.440 68.372 1.000 25.674  ? 152 GLU   BBB CA  1 ? 
ATOM   3232 C  C   . GLU   B 1 153 ? 6.279   41.845 67.176 1.000 20.968  ? 152 GLU   BBB C   1 ? 
ATOM   3233 O  O   . GLU   B 1 153 ? 7.511   41.545 67.153 1.000 23.787  ? 152 GLU   BBB O   1 ? 
ATOM   3234 C  CB  . GLU   B 1 153 ? 5.594   42.437 69.514 1.000 32.875  ? 152 GLU   BBB CB  1 ? 
ATOM   3235 C  CG  . GLU   B 1 153 ? 4.721   42.202 70.732 1.000 46.211  ? 152 GLU   BBB CG  1 ? 
ATOM   3236 C  CD  . GLU   B 1 153 ? 3.220   42.195 70.502 1.000 59.331  ? 152 GLU   BBB CD  1 ? 
ATOM   3237 O  OE1 . GLU   B 1 153 ? 2.731   43.094 69.796 1.000 66.660  ? 152 GLU   BBB OE1 1 ? 
ATOM   3238 O  OE2 . GLU   B 1 153 ? 2.542   41.282 71.031 1.000 83.004  ? 152 GLU   BBB OE2 1 ? 
ATOM   3239 N  N   . ALA   B 1 154 ? 5.687   42.558 66.215 1.000 23.042  ? 153 ALA   BBB N   1 ? 
ATOM   3240 C  CA  . ALA   B 1 154 ? 6.436   43.186 65.110 1.000 22.308  ? 153 ALA   BBB CA  1 ? 
ATOM   3241 C  C   . ALA   B 1 154 ? 7.563   44.018 65.711 1.000 23.468  ? 153 ALA   BBB C   1 ? 
ATOM   3242 O  O   . ALA   B 1 154 ? 7.367   44.659 66.763 1.000 25.150  ? 153 ALA   BBB O   1 ? 
ATOM   3243 C  CB  . ALA   B 1 154 ? 5.543   44.037 64.240 1.000 23.232  ? 153 ALA   BBB CB  1 ? 
ATOM   3244 N  N   . ASN   B 1 155 ? 8.699   44.002 65.035 1.000 20.645  ? 154 ASN   BBB N   1 ? 
ATOM   3245 C  CA  . ASN   B 1 155 ? 9.902   44.740 65.458 1.000 22.301  ? 154 ASN   BBB CA  1 ? 
ATOM   3246 C  C   . ASN   B 1 155 ? 10.018  45.937 64.535 1.000 21.491  ? 154 ASN   BBB C   1 ? 
ATOM   3247 O  O   . ASN   B 1 155 ? 10.315  45.783 63.358 1.000 21.243  ? 154 ASN   BBB O   1 ? 
ATOM   3248 C  CB  . ASN   B 1 155 ? 11.157  43.890 65.331 1.000 22.475  ? 154 ASN   BBB CB  1 ? 
ATOM   3249 C  CG  . ASN   B 1 155 ? 12.409  44.533 65.873 1.000 20.174  ? 154 ASN   BBB CG  1 ? 
ATOM   3250 O  OD1 . ASN   B 1 155 ? 12.526  45.787 65.874 1.000 28.086  ? 154 ASN   BBB OD1 1 ? 
ATOM   3251 N  ND2 . ASN   B 1 155 ? 13.388  43.706 66.236 1.000 20.933  ? 154 ASN   BBB ND2 1 ? 
ATOM   3252 N  N   . PRO   B 1 156 ? 9.696   47.156 65.020 1.000 24.065  ? 155 PRO   BBB N   1 ? 
ATOM   3253 C  CA  . PRO   B 1 156 ? 9.710   48.325 64.138 1.000 24.888  ? 155 PRO   BBB CA  1 ? 
ATOM   3254 C  C   . PRO   B 1 156 ? 11.115  48.704 63.648 1.000 24.824  ? 155 PRO   BBB C   1 ? 
ATOM   3255 O  O   . PRO   B 1 156 ? 11.217  49.316 62.587 1.000 25.230  ? 155 PRO   BBB O   1 ? 
ATOM   3256 C  CB  . PRO   B 1 156 ? 9.089   49.409 65.024 1.000 32.265  ? 155 PRO   BBB CB  1 ? 
ATOM   3257 C  CG  . PRO   B 1 156 ? 9.356   48.967 66.435 1.000 32.930  ? 155 PRO   BBB CG  1 ? 
ATOM   3258 C  CD  . PRO   B 1 156 ? 9.277   47.443 66.396 1.000 26.595  ? 155 PRO   BBB CD  1 ? 
ATOM   3259 N  N   . LYS   B 1 157 ? 12.169  48.238 64.347 1.000 23.077  ? 156 LYS   BBB N   1 ? 
ATOM   3260 C  CA  . LYS   B 1 157 ? 13.578  48.478 63.948 1.000 25.158  ? 156 LYS   BBB CA  1 ? 
ATOM   3261 C  C   . LYS   B 1 157 ? 13.852  47.846 62.575 1.000 22.320  ? 156 LYS   BBB C   1 ? 
ATOM   3262 O  O   . LYS   B 1 157 ? 14.841  48.235 61.910 1.000 23.977  ? 156 LYS   BBB O   1 ? 
ATOM   3263 C  CB  . LYS   B 1 157 ? 14.529  47.919 65.012 1.000 27.241  ? 156 LYS   BBB CB  1 ? 
ATOM   3264 C  CG  . LYS   B 1 157 ? 14.312  48.453 66.419 1.000 35.444  ? 156 LYS   BBB CG  1 ? 
ATOM   3265 C  CD  . LYS   B 1 157 ? 14.867  49.839 66.610 1.000 38.130  ? 156 LYS   BBB CD  1 ? 
ATOM   3266 C  CE  . LYS   B 1 157 ? 14.982  50.200 68.076 1.000 47.661  ? 156 LYS   BBB CE  1 ? 
ATOM   3267 N  NZ  . LYS   B 1 157 ? 16.065  49.430 68.740 1.000 46.378  ? 156 LYS   BBB NZ  1 ? 
ATOM   3268 N  N   . LEU   B 1 158 ? 13.076  46.808 62.210 1.000 23.188  ? 157 LEU   BBB N   1 ? 
ATOM   3269 C  CA  . LEU   B 1 158 ? 13.208  46.101 60.903 1.000 21.409  ? 157 LEU   BBB CA  1 ? 
ATOM   3270 C  C   . LEU   B 1 158 ? 12.577  46.851 59.726 1.000 24.761  ? 157 LEU   BBB C   1 ? 
ATOM   3271 O  O   . LEU   B 1 158 ? 12.789  46.407 58.586 1.000 21.884  ? 157 LEU   BBB O   1 ? 
ATOM   3272 C  CB  . LEU   B 1 158 ? 12.535  44.747 61.053 1.000 22.536  ? 157 LEU   BBB CB  1 ? 
ATOM   3273 C  CG  . LEU   B 1 158 ? 13.237  43.808 62.000 1.000 21.121  ? 157 LEU   BBB CG  1 ? 
ATOM   3274 C  CD1 . LEU   B 1 158 ? 12.541  42.459 61.929 1.000 24.244  ? 157 LEU   BBB CD1 1 ? 
ATOM   3275 C  CD2 . LEU   B 1 158 ? 14.696  43.675 61.645 1.000 24.852  ? 157 LEU   BBB CD2 1 ? 
ATOM   3276 N  N   . GLN   B 1 159 ? 11.877  47.961 59.989 1.000 29.776  ? 158 GLN   BBB N   1 ? 
ATOM   3277 C  CA  . GLN   B 1 159 ? 11.011  48.623 58.977 1.000 33.410  ? 158 GLN   BBB CA  1 ? 
ATOM   3278 C  C   . GLN   B 1 159 ? 11.809  49.017 57.731 1.000 27.802  ? 158 GLN   BBB C   1 ? 
ATOM   3279 O  O   . GLN   B 1 159 ? 11.338  48.692 56.609 1.000 28.561  ? 158 GLN   BBB O   1 ? 
ATOM   3280 C  CB  . GLN   B 1 159 ? 10.330  49.868 59.539 1.000 38.945  ? 158 GLN   BBB CB  1 ? 
ATOM   3281 C  CG  . GLN   B 1 159 ? 9.209   50.397 58.645 1.000 41.017  ? 158 GLN   BBB CG  1 ? 
ATOM   3282 C  CD  . GLN   B 1 159 ? 8.114   49.370 58.492 1.000 52.881  ? 158 GLN   BBB CD  1 ? 
ATOM   3283 O  OE1 . GLN   B 1 159 ? 7.508   48.923 59.466 1.000 72.071  ? 158 GLN   BBB OE1 1 ? 
ATOM   3284 N  NE2 . GLN   B 1 159 ? 7.898   48.933 57.263 1.000 57.694  ? 158 GLN   BBB NE2 1 ? 
ATOM   3285 N  N   . LYS   B 1 160 ? 12.939  49.713 57.896 1.000 24.520  ? 159 LYS   BBB N   1 ? 
ATOM   3286 C  CA  . LYS   B 1 160 ? 13.685  50.257 56.722 1.000 26.147  ? 159 LYS   BBB CA  1 ? 
ATOM   3287 C  C   . LYS   B 1 160 ? 14.124  49.053 55.886 1.000 21.941  ? 159 LYS   BBB C   1 ? 
ATOM   3288 O  O   . LYS   B 1 160 ? 14.000  49.106 54.652 1.000 24.520  ? 159 LYS   BBB O   1 ? 
ATOM   3289 C  CB  . LYS   B 1 160 ? 14.884  51.145 57.090 1.000 32.606  ? 159 LYS   BBB CB  1 ? 
ATOM   3290 C  CG  . LYS   B 1 160 ? 15.518  51.877 55.897 1.000 35.993  ? 159 LYS   BBB CG  1 ? 
ATOM   3291 C  CD  . LYS   B 1 160 ? 16.913  52.409 56.222 1.000 37.861  ? 159 LYS   BBB CD  1 ? 
ATOM   3292 C  CE  . LYS   B 1 160 ? 17.737  52.831 55.025 1.000 33.415  ? 159 LYS   BBB CE  1 ? 
ATOM   3293 N  NZ  . LYS   B 1 160 ? 17.200  54.050 54.408 1.000 45.456  ? 159 LYS   BBB NZ  1 ? 
ATOM   3294 N  N   . VAL   B 1 161 ? 14.540  47.953 56.547 1.000 22.203  ? 160 VAL   BBB N   1 ? 
ATOM   3295 C  CA  . VAL   B 1 161 ? 15.045  46.770 55.810 1.000 22.883  ? 160 VAL   BBB CA  1 ? 
ATOM   3296 C  C   . VAL   B 1 161 ? 13.883  46.130 55.000 1.000 19.652  ? 160 VAL   BBB C   1 ? 
ATOM   3297 O  O   . VAL   B 1 161 ? 14.015  45.875 53.760 1.000 22.731  ? 160 VAL   BBB O   1 ? 
ATOM   3298 C  CB  . VAL   B 1 161 ? 15.675  45.762 56.780 1.000 22.863  ? 160 VAL   BBB CB  1 ? 
ATOM   3299 C  CG1 . VAL   B 1 161 ? 16.085  44.582 55.964 1.000 29.049  ? 160 VAL   BBB CG1 1 ? 
ATOM   3300 C  CG2 . VAL   B 1 161 ? 16.868  46.310 57.550 1.000 25.390  ? 160 VAL   BBB CG2 1 ? 
ATOM   3301 N  N   . LEU   B 1 162 ? 12.761  45.891 55.695 1.000 19.954  ? 161 LEU   BBB N   1 ? 
ATOM   3302 C  CA  . LEU   B 1 162 ? 11.606  45.190 55.070 1.000 25.904  ? 161 LEU   BBB CA  1 ? 
ATOM   3303 C  C   . LEU   B 1 162 ? 11.025  46.023 53.918 1.000 21.775  ? 161 LEU   BBB C   1 ? 
ATOM   3304 O  O   . LEU   B 1 162 ? 10.666  45.475 52.875 1.000 23.418  ? 161 LEU   BBB O   1 ? 
ATOM   3305 C  CB  . LEU   B 1 162 ? 10.559  44.871 56.140 1.000 29.729  ? 161 LEU   BBB CB  1 ? 
ATOM   3306 C  CG  . LEU   B 1 162 ? 11.040  43.928 57.243 1.000 25.308  ? 161 LEU   BBB CG  1 ? 
ATOM   3307 C  CD1 . LEU   B 1 162 ? 10.077  43.970 58.426 1.000 34.494  ? 161 LEU   BBB CD1 1 ? 
ATOM   3308 C  CD2 . LEU   B 1 162 ? 11.200  42.495 56.771 1.000 29.782  ? 161 LEU   BBB CD2 1 ? 
ATOM   3309 N  N   . ASP   B 1 163 ? 10.983  47.345 54.078 1.000 21.069  ? 162 ASP   BBB N   1 ? 
ATOM   3310 C  CA  . ASP   B 1 163 ? 10.427  48.258 53.049 1.000 23.311  ? 162 ASP   BBB CA  1 ? 
ATOM   3311 C  C   . ASP   B 1 163 ? 11.314  48.214 51.798 1.000 21.427  ? 162 ASP   BBB C   1 ? 
ATOM   3312 O  O   . ASP   B 1 163 ? 10.783  48.447 50.716 1.000 25.560  ? 162 ASP   BBB O   1 ? 
ATOM   3313 C  CB  . ASP   B 1 163 ? 10.326  49.705 53.581 1.000 23.379  ? 162 ASP   BBB CB  1 ? 
ATOM   3314 C  CG  . ASP   B 1 163 ? 9.239   49.964 54.606 1.000 27.795  ? 162 ASP   BBB CG  1 ? 
ATOM   3315 O  OD1 . ASP   B 1 163 ? 8.363   49.076 54.764 1.000 31.661  ? 162 ASP   BBB OD1 1 ? 
ATOM   3316 O  OD2 . ASP   B 1 163 ? 9.212   51.127 55.178 1.000 35.412  ? 162 ASP   BBB OD2 1 ? 
ATOM   3317 N  N   . ALA   B 1 164 ? 12.620  47.913 51.947 1.000 19.927  ? 163 ALA   BBB N   1 ? 
ATOM   3318 C  CA  . ALA   B 1 164 ? 13.599  47.931 50.830 1.000 20.771  ? 163 ALA   BBB CA  1 ? 
ATOM   3319 C  C   . ALA   B 1 164 ? 13.451  46.675 49.963 1.000 21.548  ? 163 ALA   BBB C   1 ? 
ATOM   3320 O  O   . ALA   B 1 164 ? 13.941  46.663 48.795 1.000 23.411  ? 163 ALA   BBB O   1 ? 
ATOM   3321 C  CB  . ALA   B 1 164 ? 14.996  48.021 51.368 1.000 22.026  ? 163 ALA   BBB CB  1 ? 
ATOM   3322 N  N   . LEU   B 1 165 ? 12.791  45.649 50.493 1.000 21.450  ? 164 LEU   BBB N   1 ? 
ATOM   3323 C  CA  . LEU   B 1 165 ? 12.832  44.309 49.825 1.000 20.558  ? 164 LEU   BBB CA  1 ? 
ATOM   3324 C  C   . LEU   B 1 165 ? 12.066  44.354 48.493 1.000 19.538  ? 164 LEU   BBB C   1 ? 
ATOM   3325 O  O   . LEU   B 1 165 ? 12.448  43.619 47.579 1.000 21.727  ? 164 LEU   BBB O   1 ? 
ATOM   3326 C  CB  . LEU   B 1 165 ? 12.216  43.268 50.751 1.000 21.736  ? 164 LEU   BBB CB  1 ? 
ATOM   3327 C  CG  . LEU   B 1 165 ? 13.002  42.974 52.019 1.000 21.549  ? 164 LEU   BBB CG  1 ? 
ATOM   3328 C  CD1 . LEU   B 1 165 ? 12.359  41.859 52.785 1.000 23.125  ? 164 LEU   BBB CD1 1 ? 
ATOM   3329 C  CD2 . LEU   B 1 165 ? 14.455  42.697 51.719 1.000 22.924  ? 164 LEU   BBB CD2 1 ? 
ATOM   3330 N  N   . GLN   B 1 166 ? 11.052  45.225 48.351 1.000 20.602  ? 165 GLN   BBB N   1 ? 
ATOM   3331 C  CA  . GLN   B 1 166 ? 10.247  45.289 47.100 1.000 21.784  ? 165 GLN   BBB CA  1 ? 
ATOM   3332 C  C   . GLN   B 1 166 ? 11.123  45.691 45.900 1.000 20.336  ? 165 GLN   BBB C   1 ? 
ATOM   3333 O  O   . GLN   B 1 166 ? 10.719  45.387 44.766 1.000 24.727  ? 165 GLN   BBB O   1 ? 
ATOM   3334 C  CB  . GLN   B 1 166 ? 9.012   46.180 47.227 1.000 26.433  ? 165 GLN   BBB CB  1 ? 
ATOM   3335 C  CG  . GLN   B 1 166 ? 9.285   47.508 47.907 1.000 27.806  ? 165 GLN   BBB CG  1 ? 
ATOM   3336 C  CD  . GLN   B 1 166 ? 10.159  48.468 47.121 1.000 33.453  ? 165 GLN   BBB CD  1 ? 
ATOM   3337 O  OE1 . GLN   B 1 166 ? 10.020  48.638 45.886 1.000 27.407  ? 165 GLN   BBB OE1 1 ? 
ATOM   3338 N  NE2 . GLN   B 1 166 ? 11.038  49.153 47.850 1.000 33.896  ? 165 GLN   BBB NE2 1 ? 
ATOM   3339 N  N   . ALA   B 1 167 ? 12.266  46.356 46.130 1.000 23.104  ? 166 ALA   BBB N   1 ? 
ATOM   3340 C  CA  . ALA   B 1 167 ? 13.171  46.808 45.050 1.000 21.582  ? 166 ALA   BBB CA  1 ? 
ATOM   3341 C  C   . ALA   B 1 167 ? 14.178  45.702 44.693 1.000 22.207  ? 166 ALA   BBB C   1 ? 
ATOM   3342 O  O   . ALA   B 1 167 ? 14.895  45.859 43.689 1.000 21.362  ? 166 ALA   BBB O   1 ? 
ATOM   3343 C  CB  . ALA   B 1 167 ? 13.860  48.114 45.432 1.000 23.348  ? 166 ALA   BBB CB  1 ? 
ATOM   3344 N  N   . ILE   B 1 168 ? 14.240  44.609 45.462 1.000 22.395  ? 167 ILE   BBB N   1 ? 
ATOM   3345 C  CA  . ILE   B 1 168 ? 15.256  43.544 45.225 1.000 19.779  ? 167 ILE   BBB CA  1 ? 
ATOM   3346 C  C   . ILE   B 1 168 ? 14.607  42.143 45.221 1.000 18.561  ? 167 ILE   BBB C   1 ? 
ATOM   3347 O  O   . ILE   B 1 168 ? 15.183  41.229 45.865 1.000 20.152  ? 167 ILE   BBB O   1 ? 
ATOM   3348 C  CB  . ILE   B 1 168 ? 16.429  43.635 46.223 1.000 19.985  ? 167 ILE   BBB CB  1 ? 
ATOM   3349 C  CG1 . ILE   B 1 168 ? 16.011  43.469 47.682 1.000 20.031  ? 167 ILE   BBB CG1 1 ? 
ATOM   3350 C  CG2 . ILE   B 1 168 ? 17.215  44.927 46.032 1.000 20.976  ? 167 ILE   BBB CG2 1 ? 
ATOM   3351 C  CD1 . ILE   B 1 168 ? 17.081  42.805 48.513 1.000 21.023  ? 167 ILE   BBB CD1 1 ? 
ATOM   3352 N  N   . LYS   B 1 169 ? 13.508  41.953 44.497 1.000 19.377  ? 168 LYS   BBB N   1 ? 
ATOM   3353 C  CA  . LYS   B 1 169 ? 12.666  40.761 44.690 1.000 21.108  ? 168 LYS   BBB CA  1 ? 
ATOM   3354 C  C   . LYS   B 1 169 ? 13.413  39.529 44.161 1.000 21.373  ? 168 LYS   BBB C   1 ? 
ATOM   3355 O  O   . LYS   B 1 169 ? 13.194  38.426 44.738 1.000 20.737  ? 168 LYS   BBB O   1 ? 
ATOM   3356 C  CB  . LYS   B 1 169 ? 11.297  40.932 44.036 1.000 24.700  ? 168 LYS   BBB CB  1 ? 
ATOM   3357 C  CG  . LYS   B 1 169 ? 10.284  41.553 44.976 1.000 31.899  ? 168 LYS   BBB CG  1 ? 
ATOM   3358 C  CD  . LYS   B 1 169 ? 9.893   40.613 46.108 1.000 38.127  ? 168 LYS   BBB CD  1 ? 
ATOM   3359 C  CE  . LYS   B 1 169 ? 8.656   41.083 46.828 1.000 47.044  ? 168 LYS   BBB CE  1 ? 
ATOM   3360 N  NZ  . LYS   B 1 169 ? 8.533   40.410 48.136 1.000 53.356  ? 168 LYS   BBB NZ  1 ? 
ATOM   3361 N  N   . THR   B 1 170 ? 14.192  39.692 43.093 1.000 18.842  ? 169 THR   BBB N   1 ? 
ATOM   3362 C  CA  . THR   B 1 170 ? 14.824  38.565 42.372 1.000 20.407  ? 169 THR   BBB CA  1 ? 
ATOM   3363 C  C   . THR   B 1 170 ? 16.343  38.604 42.450 1.000 22.616  ? 169 THR   BBB C   1 ? 
ATOM   3364 O  O   . THR   B 1 170 ? 16.950  39.657 42.686 1.000 20.993  ? 169 THR   BBB O   1 ? 
ATOM   3365 C  CB  . THR   B 1 170 ? 14.342  38.484 40.917 1.000 21.636  ? 169 THR   BBB CB  1 ? 
ATOM   3366 O  OG1 . THR   B 1 170 ? 14.569  39.720 40.247 1.000 22.869  ? 169 THR   BBB OG1 1 ? 
ATOM   3367 C  CG2 . THR   B 1 170 ? 12.876  38.121 40.817 1.000 24.170  ? 169 THR   BBB CG2 1 ? 
ATOM   3368 N  N   . LYS   B 1 171 ? 16.941  37.439 42.217 1.000 20.658  ? 170 LYS   BBB N   1 ? 
ATOM   3369 C  CA  . LYS   B 1 171 ? 18.384  37.209 42.364 1.000 20.811  ? 170 LYS   BBB CA  1 ? 
ATOM   3370 C  C   . LYS   B 1 171 ? 19.155  38.197 41.501 1.000 20.941  ? 170 LYS   BBB C   1 ? 
ATOM   3371 O  O   . LYS   B 1 171 ? 18.853  38.281 40.291 1.000 21.621  ? 170 LYS   BBB O   1 ? 
ATOM   3372 C  CB  . LYS   B 1 171 ? 18.758  35.806 41.914 1.000 23.004  ? 170 LYS   BBB CB  1 ? 
ATOM   3373 C  CG  . LYS   B 1 171 ? 20.231  35.509 42.144 1.000 23.367  ? 170 LYS   BBB CG  1 ? 
ATOM   3374 C  CD  . LYS   B 1 171 ? 20.566  34.081 41.836 1.000 26.737  ? 170 LYS   BBB CD  1 ? 
ATOM   3375 C  CE  . LYS   B 1 171 ? 22.051  33.843 41.961 1.000 33.930  ? 170 LYS   BBB CE  1 ? 
ATOM   3376 N  NZ  . LYS   B 1 171 ? 22.303  32.395 41.943 1.000 45.257  ? 170 LYS   BBB NZ  1 ? 
ATOM   3377 N  N   . GLY   B 1 172 ? 20.102  38.908 42.118 1.000 20.240  ? 171 GLY   BBB N   1 ? 
ATOM   3378 C  CA  . GLY   B 1 172 ? 20.994  39.818 41.388 1.000 22.249  ? 171 GLY   BBB CA  1 ? 
ATOM   3379 C  C   . GLY   B 1 172 ? 20.489  41.253 41.463 1.000 21.259  ? 171 GLY   BBB C   1 ? 
ATOM   3380 O  O   . GLY   B 1 172 ? 21.289  42.173 41.166 1.000 23.987  ? 171 GLY   BBB O   1 ? 
ATOM   3381 N  N   . LYS   B 1 173 ? 19.241  41.474 41.853 1.000 18.050  ? 172 LYS   BBB N   1 ? 
ATOM   3382 C  CA  . LYS   B 1 173 ? 18.764  42.875 42.001 1.000 20.048  ? 172 LYS   BBB CA  1 ? 
ATOM   3383 C  C   . LYS   B 1 173 ? 19.425  43.525 43.213 1.000 18.712  ? 172 LYS   BBB C   1 ? 
ATOM   3384 O  O   . LYS   B 1 173 ? 19.678  42.874 44.235 1.000 19.080  ? 172 LYS   BBB O   1 ? 
ATOM   3385 C  CB  . LYS   B 1 173 ? 17.241  42.970 42.054 1.000 19.178  ? 172 LYS   BBB CB  1 ? 
ATOM   3386 C  CG  . LYS   B 1 173 ? 16.571  42.768 40.706 1.000 26.214  ? 172 LYS   BBB CG  1 ? 
ATOM   3387 C  CD  . LYS   B 1 173 ? 15.172  43.333 40.589 1.000 32.089  ? 172 LYS   BBB CD  1 ? 
ATOM   3388 C  CE  . LYS   B 1 173 ? 15.197  44.832 40.394 1.000 34.229  ? 172 LYS   BBB CE  1 ? 
ATOM   3389 N  NZ  . LYS   B 1 173 ? 13.877  45.435 40.671 1.000 35.882  ? 172 LYS   BBB NZ  1 ? 
ATOM   3390 N  N   . ARG   B 1 174 ? 19.643  44.849 43.097 1.000 20.045  ? 173 ARG   BBB N   1 ? 
ATOM   3391 C  CA  A ARG   B 1 174 ? 20.323  45.655 44.135 0.500 19.223  ? 173 ARG   BBB CA  1 ? 
ATOM   3392 C  CA  B ARG   B 1 174 ? 20.290  45.638 44.173 0.500 18.393  ? 173 ARG   BBB CA  1 ? 
ATOM   3393 C  C   . ARG   B 1 174 ? 19.725  47.067 44.150 1.000 19.038  ? 173 ARG   BBB C   1 ? 
ATOM   3394 O  O   . ARG   B 1 174 ? 19.216  47.499 43.107 1.000 22.546  ? 173 ARG   BBB O   1 ? 
ATOM   3395 C  CB  A ARG   B 1 174 ? 21.807  45.771 43.812 0.500 22.147  ? 173 ARG   BBB CB  1 ? 
ATOM   3396 C  CB  B ARG   B 1 174 ? 21.817  45.596 44.048 0.500 19.017  ? 173 ARG   BBB CB  1 ? 
ATOM   3397 C  CG  A ARG   B 1 174 ? 22.084  46.392 42.449 0.500 27.710  ? 173 ARG   BBB CG  1 ? 
ATOM   3398 C  CG  B ARG   B 1 174 ? 22.418  46.440 42.926 0.500 19.088  ? 173 ARG   BBB CG  1 ? 
ATOM   3399 C  CD  A ARG   B 1 174 ? 23.271  45.721 41.795 0.500 33.521  ? 173 ARG   BBB CD  1 ? 
ATOM   3400 C  CD  B ARG   B 1 174 ? 23.771  45.952 42.418 0.500 17.770  ? 173 ARG   BBB CD  1 ? 
ATOM   3401 N  NE  A ARG   B 1 174 ? 24.382  45.727 42.724 0.500 36.012  ? 173 ARG   BBB NE  1 ? 
ATOM   3402 N  NE  B ARG   B 1 174 ? 23.650  44.608 41.818 0.500 19.082  ? 173 ARG   BBB NE  1 ? 
ATOM   3403 C  CZ  A ARG   B 1 174 ? 25.421  44.910 42.665 0.500 31.813  ? 173 ARG   BBB CZ  1 ? 
ATOM   3404 C  CZ  B ARG   B 1 174 ? 24.556  43.638 41.880 0.500 20.282  ? 173 ARG   BBB CZ  1 ? 
ATOM   3405 N  NH1 A ARG   B 1 174 ? 26.377  45.016 43.570 0.500 36.962  ? 173 ARG   BBB NH1 1 ? 
ATOM   3406 N  NH1 B ARG   B 1 174 ? 24.295  42.471 41.318 0.500 20.050  ? 173 ARG   BBB NH1 1 ? 
ATOM   3407 N  NH2 A ARG   B 1 174 ? 25.518  44.021 41.690 0.500 24.506  ? 173 ARG   BBB NH2 1 ? 
ATOM   3408 N  NH2 B ARG   B 1 174 ? 25.694  43.794 42.532 0.500 22.112  ? 173 ARG   BBB NH2 1 ? 
ATOM   3409 N  N   . ALA   B 1 175 ? 19.778  47.700 45.289 1.000 20.121  ? 174 ALA   BBB N   1 ? 
ATOM   3410 C  CA  . ALA   B 1 175 ? 19.351  49.109 45.394 1.000 21.691  ? 174 ALA   BBB CA  1 ? 
ATOM   3411 C  C   . ALA   B 1 175 ? 20.220  49.804 46.422 1.000 23.440  ? 174 ALA   BBB C   1 ? 
ATOM   3412 O  O   . ALA   B 1 175 ? 20.725  49.219 47.373 1.000 21.762  ? 174 ALA   BBB O   1 ? 
ATOM   3413 C  CB  . ALA   B 1 175 ? 17.893  49.137 45.771 1.000 22.365  ? 174 ALA   BBB CB  1 ? 
ATOM   3414 N  N   . PRO   B 1 176 ? 20.384  51.133 46.276 1.000 22.183  ? 175 PRO   BBB N   1 ? 
ATOM   3415 C  CA  . PRO   B 1 176 ? 21.033  51.873 47.335 1.000 24.340  ? 175 PRO   BBB CA  1 ? 
ATOM   3416 C  C   . PRO   B 1 176 ? 20.289  51.639 48.674 1.000 24.238  ? 175 PRO   BBB C   1 ? 
ATOM   3417 O  O   . PRO   B 1 176 ? 19.058  51.644 48.702 1.000 26.254  ? 175 PRO   BBB O   1 ? 
ATOM   3418 C  CB  . PRO   B 1 176 ? 20.874  53.340 46.879 1.000 27.837  ? 175 PRO   BBB CB  1 ? 
ATOM   3419 C  CG  . PRO   B 1 176 ? 20.823  53.199 45.371 1.000 28.700  ? 175 PRO   BBB CG  1 ? 
ATOM   3420 C  CD  . PRO   B 1 176 ? 20.045  51.922 45.092 1.000 23.801  ? 175 PRO   BBB CD  1 ? 
ATOM   3421 N  N   . PHE   B 1 177 ? 21.073  51.637 49.745 1.000 22.193  ? 176 PHE   BBB N   1 ? 
ATOM   3422 C  CA  . PHE   B 1 177 ? 20.551  51.446 51.152 1.000 25.803  ? 176 PHE   BBB CA  1 ? 
ATOM   3423 C  C   . PHE   B 1 177 ? 21.458  52.268 52.059 1.000 22.566  ? 176 PHE   BBB C   1 ? 
ATOM   3424 O  O   . PHE   B 1 177 ? 22.632  51.930 52.224 1.000 29.508  ? 176 PHE   BBB O   1 ? 
ATOM   3425 C  CB  . PHE   B 1 177 ? 20.525  49.945 51.504 1.000 22.557  ? 176 PHE   BBB CB  1 ? 
ATOM   3426 C  CG  . PHE   B 1 177 ? 19.801  49.709 52.847 1.000 24.221  ? 176 PHE   BBB CG  1 ? 
ATOM   3427 C  CD1 . PHE   B 1 177 ? 20.475  49.858 54.053 1.000 24.545  ? 176 PHE   BBB CD1 1 ? 
ATOM   3428 C  CD2 . PHE   B 1 177 ? 18.456  49.367 52.852 1.000 23.174  ? 176 PHE   BBB CD2 1 ? 
ATOM   3429 C  CE1 . PHE   B 1 177 ? 19.803  49.686 55.252 1.000 23.818  ? 176 PHE   BBB CE1 1 ? 
ATOM   3430 C  CE2 . PHE   B 1 177 ? 17.788  49.143 54.054 1.000 25.426  ? 176 PHE   BBB CE2 1 ? 
ATOM   3431 C  CZ  . PHE   B 1 177 ? 18.459  49.330 55.251 1.000 22.079  ? 176 PHE   BBB CZ  1 ? 
ATOM   3432 N  N   . THR   B 1 178 ? 20.969  53.469 52.431 1.000 28.031  ? 177 THR   BBB N   1 ? 
ATOM   3433 C  CA  . THR   B 1 178 ? 21.869  54.540 52.945 1.000 25.267  ? 177 THR   BBB CA  1 ? 
ATOM   3434 C  C   . THR   B 1 178 ? 21.361  55.041 54.313 1.000 28.558  ? 177 THR   BBB C   1 ? 
ATOM   3435 O  O   . THR   B 1 178 ? 20.184  54.838 54.656 1.000 29.813  ? 177 THR   BBB O   1 ? 
ATOM   3436 C  CB  . THR   B 1 178 ? 21.990  55.741 51.993 1.000 28.400  ? 177 THR   BBB CB  1 ? 
ATOM   3437 O  OG1 . THR   B 1 178 ? 20.645  56.216 51.809 1.000 30.913  ? 177 THR   BBB OG1 1 ? 
ATOM   3438 C  CG2 . THR   B 1 178 ? 22.621  55.444 50.649 1.000 31.737  ? 177 THR   BBB CG2 1 ? 
ATOM   3439 N  N   . ASN   B 1 179 ? 22.298  55.603 55.081 1.000 33.050  ? 178 ASN   BBB N   1 ? 
ATOM   3440 C  CA  . ASN   B 1 179 ? 21.950  56.337 56.339 1.000 30.927  ? 178 ASN   BBB CA  1 ? 
ATOM   3441 C  C   . ASN   B 1 179 ? 21.271  55.347 57.294 1.000 31.460  ? 178 ASN   BBB C   1 ? 
ATOM   3442 O  O   . ASN   B 1 179 ? 20.060  55.535 57.598 1.000 29.009  ? 178 ASN   BBB O   1 ? 
ATOM   3443 C  CB  . ASN   B 1 179 ? 21.094  57.592 56.059 1.000 30.258  ? 178 ASN   BBB CB  1 ? 
ATOM   3444 C  CG  . ASN   B 1 179 ? 20.897  58.372 57.333 1.000 35.532  ? 178 ASN   BBB CG  1 ? 
ATOM   3445 O  OD1 . ASN   B 1 179 ? 19.776  58.810 57.628 1.000 47.127  ? 178 ASN   BBB OD1 1 ? 
ATOM   3446 N  ND2 . ASN   B 1 179 ? 21.980  58.518 58.099 1.000 39.405  ? 178 ASN   BBB ND2 1 ? 
ATOM   3447 N  N   . PHE   B 1 180 ? 21.997  54.287 57.676 1.000 26.798  ? 179 PHE   BBB N   1 ? 
ATOM   3448 C  CA  . PHE   B 1 180 ? 21.417  53.207 58.516 1.000 32.949  ? 179 PHE   BBB CA  1 ? 
ATOM   3449 C  C   . PHE   B 1 180 ? 22.488  52.650 59.465 1.000 30.208  ? 179 PHE   BBB C   1 ? 
ATOM   3450 O  O   . PHE   B 1 180 ? 23.587  52.306 58.908 1.000 25.451  ? 179 PHE   BBB O   1 ? 
ATOM   3451 C  CB  . PHE   B 1 180 ? 20.833  52.063 57.684 1.000 28.133  ? 179 PHE   BBB CB  1 ? 
ATOM   3452 C  CG  . PHE   B 1 180 ? 20.097  51.100 58.575 1.000 26.827  ? 179 PHE   BBB CG  1 ? 
ATOM   3453 C  CD1 . PHE   B 1 180 ? 18.849  51.427 59.082 1.000 30.119  ? 179 PHE   BBB CD1 1 ? 
ATOM   3454 C  CD2 . PHE   B 1 180 ? 20.650  49.863 58.906 1.000 25.515  ? 179 PHE   BBB CD2 1 ? 
ATOM   3455 C  CE1 . PHE   B 1 180 ? 18.180  50.586 59.946 1.000 29.947  ? 179 PHE   BBB CE1 1 ? 
ATOM   3456 C  CE2 . PHE   B 1 180 ? 19.971  49.032 59.772 1.000 24.851  ? 179 PHE   BBB CE2 1 ? 
ATOM   3457 C  CZ  . PHE   B 1 180 ? 18.736  49.359 60.263 1.000 25.260  ? 179 PHE   BBB CZ  1 ? 
ATOM   3458 N  N   . ASP   B 1 181 ? 22.152  52.565 60.787 1.000 35.985  ? 180 ASP   BBB N   1 ? 
ATOM   3459 C  CA  . ASP   B 1 181 ? 23.135  52.175 61.843 1.000 31.733  ? 180 ASP   BBB CA  1 ? 
ATOM   3460 C  C   . ASP   B 1 181 ? 22.613  50.823 62.316 1.000 24.885  ? 180 ASP   BBB C   1 ? 
ATOM   3461 O  O   . ASP   B 1 181 ? 21.604  50.826 63.044 1.000 28.933  ? 180 ASP   BBB O   1 ? 
ATOM   3462 C  CB  . ASP   B 1 181 ? 23.178  53.190 63.016 1.000 31.858  ? 180 ASP   BBB CB  1 ? 
ATOM   3463 C  CG  . ASP   B 1 181 ? 24.151  52.798 64.168 1.000 31.140  ? 180 ASP   BBB CG  1 ? 
ATOM   3464 O  OD1 . ASP   B 1 181 ? 24.586  51.565 64.215 1.000 30.638  ? 180 ASP   BBB OD1 1 ? 
ATOM   3465 O  OD2 . ASP   B 1 181 ? 24.443  53.656 65.082 1.000 39.542  ? 180 ASP   BBB OD2 1 ? 
ATOM   3466 N  N   . PRO   B 1 182 ? 23.214  49.670 61.914 1.000 26.483  ? 181 PRO   BBB N   1 ? 
ATOM   3467 C  CA  . PRO   B 1 182 ? 22.587  48.389 62.242 1.000 25.055  ? 181 PRO   BBB CA  1 ? 
ATOM   3468 C  C   . PRO   B 1 182 ? 22.720  48.096 63.748 1.000 25.279  ? 181 PRO   BBB C   1 ? 
ATOM   3469 O  O   . PRO   B 1 182 ? 22.123  47.170 64.215 1.000 25.477  ? 181 PRO   BBB O   1 ? 
ATOM   3470 C  CB  . PRO   B 1 182 ? 23.306  47.406 61.316 1.000 30.018  ? 181 PRO   BBB CB  1 ? 
ATOM   3471 C  CG  . PRO   B 1 182 ? 24.686  47.996 61.117 1.000 29.780  ? 181 PRO   BBB CG  1 ? 
ATOM   3472 C  CD  . PRO   B 1 182 ? 24.456  49.516 61.138 1.000 29.916  ? 181 PRO   BBB CD  1 ? 
ATOM   3473 N  N   . SER   B 1 183 ? 23.418  48.924 64.545 1.000 23.600  ? 182 SER   BBB N   1 ? 
ATOM   3474 C  CA  . SER   B 1 183 ? 23.447  48.703 66.019 1.000 24.031  ? 182 SER   BBB CA  1 ? 
ATOM   3475 C  C   . SER   B 1 183 ? 22.043  48.957 66.603 1.000 22.691  ? 182 SER   BBB C   1 ? 
ATOM   3476 O  O   . SER   B 1 183 ? 21.790  48.480 67.771 1.000 21.936  ? 182 SER   BBB O   1 ? 
ATOM   3477 C  CB  . SER   B 1 183 ? 24.531  49.493 66.723 1.000 25.923  ? 182 SER   BBB CB  1 ? 
ATOM   3478 O  OG  . SER   B 1 183 ? 24.184  50.848 66.756 1.000 28.281  ? 182 SER   BBB OG  1 ? 
ATOM   3479 N  N   . THR   B 1 184 ? 21.143  49.680 65.854 1.000 22.456  ? 183 THR   BBB N   1 ? 
ATOM   3480 C  CA  . THR   B 1 184 ? 19.726  49.819 66.293 1.000 22.048  ? 183 THR   BBB CA  1 ? 
ATOM   3481 C  C   . THR   B 1 184 ? 18.970  48.472 66.332 1.000 21.722  ? 183 THR   BBB C   1 ? 
ATOM   3482 O  O   . THR   B 1 184 ? 17.892  48.391 66.941 1.000 26.554  ? 183 THR   BBB O   1 ? 
ATOM   3483 C  CB  . THR   B 1 184 ? 18.958  50.718 65.333 1.000 26.730  ? 183 THR   BBB CB  1 ? 
ATOM   3484 O  OG1 . THR   B 1 184 ? 19.122  50.290 63.963 1.000 25.783  ? 183 THR   BBB OG1 1 ? 
ATOM   3485 C  CG2 . THR   B 1 184 ? 19.469  52.145 65.402 1.000 28.733  ? 183 THR   BBB CG2 1 ? 
ATOM   3486 N  N   . LEU   B 1 185 ? 19.515  47.473 65.644 1.000 20.540  ? 184 LEU   BBB N   1 ? 
ATOM   3487 C  CA  . LEU   B 1 185 ? 18.856  46.153 65.593 1.000 21.109  ? 184 LEU   BBB CA  1 ? 
ATOM   3488 C  C   . LEU   B 1 185 ? 19.246  45.329 66.812 1.000 19.277  ? 184 LEU   BBB C   1 ? 
ATOM   3489 O  O   . LEU   B 1 185 ? 18.641  44.238 66.983 1.000 23.271  ? 184 LEU   BBB O   1 ? 
ATOM   3490 C  CB  . LEU   B 1 185 ? 19.308  45.472 64.294 1.000 20.461  ? 184 LEU   BBB CB  1 ? 
ATOM   3491 C  CG  . LEU   B 1 185 ? 18.803  46.100 63.011 1.000 22.284  ? 184 LEU   BBB CG  1 ? 
ATOM   3492 C  CD1 . LEU   B 1 185 ? 19.466  45.564 61.756 1.000 28.107  ? 184 LEU   BBB CD1 1 ? 
ATOM   3493 C  CD2 . LEU   B 1 185 ? 17.307  46.040 62.916 1.000 25.511  ? 184 LEU   BBB CD2 1 ? 
ATOM   3494 N  N   . LEU   B 1 186 ? 20.318  45.653 67.503 1.000 20.258  ? 185 LEU   BBB N   1 ? 
ATOM   3495 C  CA  . LEU   B 1 186 ? 20.858  44.804 68.616 1.000 20.616  ? 185 LEU   BBB CA  1 ? 
ATOM   3496 C  C   . LEU   B 1 186 ? 19.965  44.881 69.850 1.000 20.587  ? 185 LEU   BBB C   1 ? 
ATOM   3497 O  O   . LEU   B 1 186 ? 19.254  45.862 70.102 1.000 23.486  ? 185 LEU   BBB O   1 ? 
ATOM   3498 C  CB  . LEU   B 1 186 ? 22.290  45.226 68.945 1.000 22.776  ? 185 LEU   BBB CB  1 ? 
ATOM   3499 C  CG  . LEU   B 1 186 ? 23.273  45.144 67.799 1.000 26.690  ? 185 LEU   BBB CG  1 ? 
ATOM   3500 C  CD1 . LEU   B 1 186 ? 24.643  45.625 68.245 1.000 26.601  ? 185 LEU   BBB CD1 1 ? 
ATOM   3501 C  CD2 . LEU   B 1 186 ? 23.401  43.685 67.360 1.000 27.424  ? 185 LEU   BBB CD2 1 ? 
ATOM   3502 N  N   . PRO   B 1 187 ? 20.004  43.893 70.763 1.000 26.641  ? 186 PRO   BBB N   1 ? 
ATOM   3503 C  CA  . PRO   B 1 187 ? 19.261  43.979 72.013 1.000 25.866  ? 186 PRO   BBB CA  1 ? 
ATOM   3504 C  C   . PRO   B 1 187 ? 19.809  45.127 72.904 1.000 24.072  ? 186 PRO   BBB C   1 ? 
ATOM   3505 O  O   . PRO   B 1 187 ? 20.945  45.507 72.686 1.000 22.891  ? 186 PRO   BBB O   1 ? 
ATOM   3506 C  CB  . PRO   B 1 187 ? 19.417  42.539 72.575 1.000 23.057  ? 186 PRO   BBB CB  1 ? 
ATOM   3507 C  CG  . PRO   B 1 187 ? 20.738  42.143 72.043 1.000 23.276  ? 186 PRO   BBB CG  1 ? 
ATOM   3508 C  CD  . PRO   B 1 187 ? 20.688  42.580 70.596 1.000 24.102  ? 186 PRO   BBB CD  1 ? 
ATOM   3509 N  N   . SER   B 1 188 ? 19.083  45.468 73.961 1.000 28.713  ? 187 SER   BBB N   1 ? 
ATOM   3510 C  CA  A SER   B 1 188 ? 19.485  46.580 74.886 0.500 24.935  ? 187 SER   BBB CA  1 ? 
ATOM   3511 C  CA  B SER   B 1 188 ? 19.479  46.574 74.891 0.500 24.022  ? 187 SER   BBB CA  1 ? 
ATOM   3512 C  C   . SER   B 1 188 ? 20.780  46.181 75.606 1.000 22.091  ? 187 SER   BBB C   1 ? 
ATOM   3513 O  O   . SER   B 1 188 ? 21.683  46.995 75.693 1.000 22.776  ? 187 SER   BBB O   1 ? 
ATOM   3514 C  CB  A SER   B 1 188 ? 18.409  46.883 75.890 0.500 26.366  ? 187 SER   BBB CB  1 ? 
ATOM   3515 C  CB  B SER   B 1 188 ? 18.382  46.831 75.879 0.500 23.143  ? 187 SER   BBB CB  1 ? 
ATOM   3516 O  OG  A SER   B 1 188 ? 17.226  47.353 75.256 0.500 31.371  ? 187 SER   BBB OG  1 ? 
ATOM   3517 O  OG  B SER   B 1 188 ? 18.797  47.733 76.890 0.500 23.347  ? 187 SER   BBB OG  1 ? 
ATOM   3518 N  N   . SER   B 1 189 ? 20.834  44.923 76.082 1.000 25.016  ? 188 SER   BBB N   1 ? 
ATOM   3519 C  CA  . SER   B 1 189 ? 21.996  44.315 76.786 1.000 24.474  ? 188 SER   BBB CA  1 ? 
ATOM   3520 C  C   . SER   B 1 189 ? 22.861  43.527 75.792 1.000 23.351  ? 188 SER   BBB C   1 ? 
ATOM   3521 O  O   . SER   B 1 189 ? 22.284  42.862 74.923 1.000 23.171  ? 188 SER   BBB O   1 ? 
ATOM   3522 C  CB  . SER   B 1 189 ? 21.569  43.409 77.914 1.000 29.021  ? 188 SER   BBB CB  1 ? 
ATOM   3523 O  OG  . SER   B 1 189 ? 22.715  42.769 78.468 1.000 32.477  ? 188 SER   BBB OG  1 ? 
ATOM   3524 N  N   . LEU   B 1 190 ? 24.183  43.665 75.887 1.000 24.231  ? 189 LEU   BBB N   1 ? 
ATOM   3525 C  CA  . LEU   B 1 190 ? 25.140  43.039 74.952 1.000 24.684  ? 189 LEU   BBB CA  1 ? 
ATOM   3526 C  C   . LEU   B 1 190 ? 25.942  42.006 75.735 1.000 22.529  ? 189 LEU   BBB C   1 ? 
ATOM   3527 O  O   . LEU   B 1 190 ? 27.047  41.726 75.289 1.000 22.807  ? 189 LEU   BBB O   1 ? 
ATOM   3528 C  CB  . LEU   B 1 190 ? 26.029  44.088 74.257 1.000 25.588  ? 189 LEU   BBB CB  1 ? 
ATOM   3529 C  CG  . LEU   B 1 190 ? 25.301  45.056 73.324 1.000 24.138  ? 189 LEU   BBB CG  1 ? 
ATOM   3530 C  CD1 . LEU   B 1 190 ? 26.293  45.912 72.556 1.000 29.399  ? 189 LEU   BBB CD1 1 ? 
ATOM   3531 C  CD2 . LEU   B 1 190 ? 24.369  44.334 72.357 1.000 28.683  ? 189 LEU   BBB CD2 1 ? 
ATOM   3532 N  N   . ASP   B 1 191 ? 25.384  41.437 76.817 1.000 21.928  ? 190 ASP   BBB N   1 ? 
ATOM   3533 C  CA  . ASP   B 1 191 ? 25.933  40.164 77.383 1.000 22.506  ? 190 ASP   BBB CA  1 ? 
ATOM   3534 C  C   . ASP   B 1 191 ? 26.035  39.165 76.228 1.000 19.512  ? 190 ASP   BBB C   1 ? 
ATOM   3535 O  O   . ASP   B 1 191 ? 25.124  39.158 75.374 1.000 20.648  ? 190 ASP   BBB O   1 ? 
ATOM   3536 C  CB  . ASP   B 1 191 ? 25.082  39.563 78.507 1.000 27.903  ? 190 ASP   BBB CB  1 ? 
ATOM   3537 C  CG  . ASP   B 1 191 ? 25.037  40.373 79.787 1.000 28.650  ? 190 ASP   BBB CG  1 ? 
ATOM   3538 O  OD1 . ASP   B 1 191 ? 25.975  41.177 80.008 1.000 28.142  ? 190 ASP   BBB OD1 1 ? 
ATOM   3539 O  OD2 . ASP   B 1 191 ? 24.068  40.174 80.564 1.000 32.798  ? 190 ASP   BBB OD2 1 ? 
ATOM   3540 N  N   . PHE   B 1 192 ? 27.122  38.378 76.185 1.000 19.247  ? 191 PHE   BBB N   1 ? 
ATOM   3541 C  CA  . PHE   B 1 192 ? 27.386  37.533 75.001 1.000 19.182  ? 191 PHE   BBB CA  1 ? 
ATOM   3542 C  C   . PHE   B 1 192 ? 28.114  36.250 75.400 1.000 18.037  ? 191 PHE   BBB C   1 ? 
ATOM   3543 O  O   . PHE   B 1 192 ? 28.757  36.154 76.442 1.000 19.167  ? 191 PHE   BBB O   1 ? 
ATOM   3544 C  CB  . PHE   B 1 192 ? 28.171  38.269 73.911 1.000 19.556  ? 191 PHE   BBB CB  1 ? 
ATOM   3545 C  CG  . PHE   B 1 192 ? 29.572  38.654 74.302 1.000 18.661  ? 191 PHE   BBB CG  1 ? 
ATOM   3546 C  CD1 . PHE   B 1 192 ? 29.830  39.833 75.010 1.000 20.462  ? 191 PHE   BBB CD1 1 ? 
ATOM   3547 C  CD2 . PHE   B 1 192 ? 30.655  37.857 73.968 1.000 18.367  ? 191 PHE   BBB CD2 1 ? 
ATOM   3548 C  CE1 . PHE   B 1 192 ? 31.124  40.144 75.400 1.000 20.810  ? 191 PHE   BBB CE1 1 ? 
ATOM   3549 C  CE2 . PHE   B 1 192 ? 31.938  38.175 74.354 1.000 18.886  ? 191 PHE   BBB CE2 1 ? 
ATOM   3550 C  CZ  . PHE   B 1 192 ? 32.179  39.349 75.044 1.000 20.346  ? 191 PHE   BBB CZ  1 ? 
ATOM   3551 N  N   . TRP   B 1 193 ? 27.971  35.295 74.496 1.000 17.785  ? 192 TRP   BBB N   1 ? 
ATOM   3552 C  CA  . TRP   B 1 193 ? 28.848  34.096 74.413 1.000 18.761  ? 192 TRP   BBB CA  1 ? 
ATOM   3553 C  C   . TRP   B 1 193 ? 29.788  34.255 73.226 1.000 18.210  ? 192 TRP   BBB C   1 ? 
ATOM   3554 O  O   . TRP   B 1 193 ? 29.401  34.858 72.182 1.000 19.222  ? 192 TRP   BBB O   1 ? 
ATOM   3555 C  CB  . TRP   B 1 193 ? 27.994  32.837 74.204 1.000 19.983  ? 192 TRP   BBB CB  1 ? 
ATOM   3556 C  CG  . TRP   B 1 193 ? 27.013  32.525 75.283 1.000 19.188  ? 192 TRP   BBB CG  1 ? 
ATOM   3557 C  CD1 . TRP   B 1 193 ? 27.301  32.042 76.530 1.000 21.053  ? 192 TRP   BBB CD1 1 ? 
ATOM   3558 C  CD2 . TRP   B 1 193 ? 25.583  32.612 75.213 1.000 18.925  ? 192 TRP   BBB CD2 1 ? 
ATOM   3559 N  NE1 . TRP   B 1 193 ? 26.149  31.823 77.240 1.000 21.190  ? 192 TRP   BBB NE1 1 ? 
ATOM   3560 C  CE2 . TRP   B 1 193 ? 25.077  32.177 76.463 1.000 21.383  ? 192 TRP   BBB CE2 1 ? 
ATOM   3561 C  CE3 . TRP   B 1 193 ? 24.670  33.047 74.236 1.000 19.588  ? 192 TRP   BBB CE3 1 ? 
ATOM   3562 C  CZ2 . TRP   B 1 193 ? 23.717  32.181 76.765 1.000 24.093  ? 192 TRP   BBB CZ2 1 ? 
ATOM   3563 C  CZ3 . TRP   B 1 193 ? 23.324  32.999 74.514 1.000 21.017  ? 192 TRP   BBB CZ3 1 ? 
ATOM   3564 C  CH2 . TRP   B 1 193 ? 22.853  32.543 75.759 1.000 21.788  ? 192 TRP   BBB CH2 1 ? 
ATOM   3565 N  N   . THR   B 1 194 ? 30.949  33.647 73.302 1.000 19.135  ? 193 THR   BBB N   1 ? 
ATOM   3566 C  CA  . THR   B 1 194 ? 31.873  33.664 72.150 1.000 19.831  ? 193 THR   BBB CA  1 ? 
ATOM   3567 C  C   . THR   B 1 194 ? 32.494  32.279 71.997 1.000 18.020  ? 193 THR   BBB C   1 ? 
ATOM   3568 O  O   . THR   B 1 194 ? 32.827  31.674 73.037 1.000 21.264  ? 193 THR   BBB O   1 ? 
ATOM   3569 C  CB  . THR   B 1 194 ? 32.868  34.821 72.303 1.000 21.287  ? 193 THR   BBB CB  1 ? 
ATOM   3570 O  OG1 . THR   B 1 194 ? 33.678  34.811 71.132 1.000 21.217  ? 193 THR   BBB OG1 1 ? 
ATOM   3571 C  CG2 . THR   B 1 194 ? 33.736  34.667 73.535 1.000 20.766  ? 193 THR   BBB CG2 1 ? 
ATOM   3572 N  N   . TYR   B 1 195 ? 32.763  31.935 70.745 1.000 19.333  ? 194 TYR   BBB N   1 ? 
ATOM   3573 C  CA  . TYR   B 1 195 ? 33.497  30.676 70.420 1.000 19.859  ? 194 TYR   BBB CA  1 ? 
ATOM   3574 C  C   . TYR   B 1 195 ? 34.119  30.806 69.037 1.000 20.531  ? 194 TYR   BBB C   1 ? 
ATOM   3575 O  O   . TYR   B 1 195 ? 33.690  31.633 68.217 1.000 19.612  ? 194 TYR   BBB O   1 ? 
ATOM   3576 C  CB  . TYR   B 1 195 ? 32.528  29.502 70.516 1.000 20.186  ? 194 TYR   BBB CB  1 ? 
ATOM   3577 C  CG  . TYR   B 1 195 ? 31.608  29.395 69.332 1.000 19.290  ? 194 TYR   BBB CG  1 ? 
ATOM   3578 C  CD1 . TYR   B 1 195 ? 30.406  30.078 69.269 1.000 21.087  ? 194 TYR   BBB CD1 1 ? 
ATOM   3579 C  CD2 . TYR   B 1 195 ? 31.935  28.607 68.245 1.000 21.131  ? 194 TYR   BBB CD2 1 ? 
ATOM   3580 C  CE1 . TYR   B 1 195 ? 29.591  30.026 68.151 1.000 20.140  ? 194 TYR   BBB CE1 1 ? 
ATOM   3581 C  CE2 . TYR   B 1 195 ? 31.110  28.500 67.139 1.000 20.412  ? 194 TYR   BBB CE2 1 ? 
ATOM   3582 C  CZ  . TYR   B 1 195 ? 29.950  29.276 67.048 1.000 18.224  ? 194 TYR   BBB CZ  1 ? 
ATOM   3583 O  OH  . TYR   B 1 195 ? 29.137  29.195 65.951 1.000 20.424  ? 194 TYR   BBB OH  1 ? 
ATOM   3584 N  N   . PRO   B 1 196 ? 35.172  30.011 68.743 1.000 20.972  ? 195 PRO   BBB N   1 ? 
ATOM   3585 C  CA  . PRO   B 1 196 ? 35.831  30.063 67.443 1.000 21.623  ? 195 PRO   BBB CA  1 ? 
ATOM   3586 C  C   . PRO   B 1 196 ? 35.064  29.183 66.465 1.000 21.230  ? 195 PRO   BBB C   1 ? 
ATOM   3587 O  O   . PRO   B 1 196 ? 34.809  27.983 66.779 1.000 25.302  ? 195 PRO   BBB O   1 ? 
ATOM   3588 C  CB  . PRO   B 1 196 ? 37.254  29.565 67.750 1.000 22.608  ? 195 PRO   BBB CB  1 ? 
ATOM   3589 C  CG  . PRO   B 1 196 ? 37.000  28.553 68.849 1.000 26.263  ? 195 PRO   BBB CG  1 ? 
ATOM   3590 C  CD  . PRO   B 1 196 ? 35.935  29.212 69.708 1.000 22.565  ? 195 PRO   BBB CD  1 ? 
ATOM   3591 N  N   . GLY   B 1 197 ? 34.761  29.700 65.294 1.000 20.106  ? 196 GLY   BBB N   1 ? 
ATOM   3592 C  CA  . GLY   B 1 197 ? 33.879  29.047 64.316 1.000 21.094  ? 196 GLY   BBB CA  1 ? 
ATOM   3593 C  C   . GLY   B 1 197 ? 34.185  29.466 62.883 1.000 19.798  ? 196 GLY   BBB C   1 ? 
ATOM   3594 O  O   . GLY   B 1 197 ? 35.347  29.751 62.543 1.000 23.466  ? 196 GLY   BBB O   1 ? 
ATOM   3595 N  N   . SER   B 1 198 ? 33.155  29.336 62.059 1.000 20.699  ? 197 SER   BBB N   1 ? 
ATOM   3596 C  CA  . SER   B 1 198 ? 33.252  29.360 60.586 1.000 21.299  ? 197 SER   BBB CA  1 ? 
ATOM   3597 C  C   . SER   B 1 198 ? 32.147  30.295 60.069 1.000 17.966  ? 197 SER   BBB C   1 ? 
ATOM   3598 O  O   . SER   B 1 198 ? 31.152  30.534 60.796 1.000 19.396  ? 197 SER   BBB O   1 ? 
ATOM   3599 C  CB  . SER   B 1 198 ? 33.133  27.928 59.999 1.000 22.801  ? 197 SER   BBB CB  1 ? 
ATOM   3600 O  OG  . SER   B 1 198 ? 31.774  27.519 60.005 1.000 21.808  ? 197 SER   BBB OG  1 ? 
ATOM   3601 N  N   . LEU   B 1 199 ? 32.255  30.615 58.790 1.000 18.112  ? 198 LEU   BBB N   1 ? 
ATOM   3602 C  CA  . LEU   B 1 199 ? 31.105  31.054 57.980 1.000 19.635  ? 198 LEU   BBB CA  1 ? 
ATOM   3603 C  C   . LEU   B 1 199 ? 30.040  29.961 58.031 1.000 17.821  ? 198 LEU   BBB C   1 ? 
ATOM   3604 O  O   . LEU   B 1 199 ? 30.468  28.738 57.994 1.000 20.378  ? 198 LEU   BBB O   1 ? 
ATOM   3605 C  CB  . LEU   B 1 199 ? 31.593  31.260 56.552 1.000 19.397  ? 198 LEU   BBB CB  1 ? 
ATOM   3606 C  CG  . LEU   B 1 199 ? 32.647  32.378 56.396 1.000 21.010  ? 198 LEU   BBB CG  1 ? 
ATOM   3607 C  CD1 . LEU   B 1 199 ? 33.098  32.477 54.951 1.000 26.967  ? 198 LEU   BBB CD1 1 ? 
ATOM   3608 C  CD2 . LEU   B 1 199 ? 32.189  33.692 56.977 1.000 22.041  ? 198 LEU   BBB CD2 1 ? 
ATOM   3609 N  N   . THR   B 1 200 ? 28.759  30.262 58.122 1.000 17.393  ? 199 THR   BBB N   1 ? 
ATOM   3610 C  CA  . THR   B 1 200 ? 27.706  29.211 58.218 1.000 18.622  ? 199 THR   BBB CA  1 ? 
ATOM   3611 C  C   . THR   B 1 200 ? 27.230  28.772 56.832 1.000 19.295  ? 199 THR   BBB C   1 ? 
ATOM   3612 O  O   . THR   B 1 200 ? 26.287  27.915 56.751 1.000 21.274  ? 199 THR   BBB O   1 ? 
ATOM   3613 C  CB  . THR   B 1 200 ? 26.506  29.665 59.050 1.000 18.795  ? 199 THR   BBB CB  1 ? 
ATOM   3614 O  OG1 . THR   B 1 200 ? 25.828  30.747 58.374 1.000 21.608  ? 199 THR   BBB OG1 1 ? 
ATOM   3615 C  CG2 . THR   B 1 200 ? 26.945  29.990 60.463 1.000 19.424  ? 199 THR   BBB CG2 1 ? 
ATOM   3616 N  N   . HIS   B 1 201 ? 27.873  29.209 55.774 1.000 23.508  ? 200 HIS   BBB N   1 ? 
ATOM   3617 C  CA  . HIS   B 1 201 ? 27.556  28.736 54.410 1.000 20.575  ? 200 HIS   BBB CA  1 ? 
ATOM   3618 C  C   . HIS   B 1 201 ? 28.846  28.808 53.617 1.000 18.019  ? 200 HIS   BBB C   1 ? 
ATOM   3619 O  O   . HIS   B 1 201 ? 29.819  29.439 54.075 1.000 20.926  ? 200 HIS   BBB O   1 ? 
ATOM   3620 C  CB  . HIS   B 1 201 ? 26.281  29.350 53.813 1.000 22.100  ? 200 HIS   BBB CB  1 ? 
ATOM   3621 C  CG  . HIS   B 1 201 ? 26.422  30.830 53.530 1.000 20.099  ? 200 HIS   BBB CG  1 ? 
ATOM   3622 N  ND1 . HIS   B 1 201 ? 25.629  31.864 54.068 1.000 24.735  ? 200 HIS   BBB ND1 1 ? 
ATOM   3623 C  CD2 . HIS   B 1 201 ? 27.287  31.396 52.677 1.000 18.558  ? 200 HIS   BBB CD2 1 ? 
ATOM   3624 C  CE1 . HIS   B 1 201 ? 26.016  33.015 53.524 1.000 20.195  ? 200 HIS   BBB CE1 1 ? 
ATOM   3625 N  NE2 . HIS   B 1 201 ? 27.038  32.768 52.673 1.000 23.369  ? 200 HIS   BBB NE2 1 ? 
ATOM   3626 N  N   . PRO   B 1 202 ? 28.910  28.143 52.439 1.000 20.131  ? 201 PRO   BBB N   1 ? 
ATOM   3627 C  CA  . PRO   B 1 202 ? 30.115  28.201 51.621 1.000 21.087  ? 201 PRO   BBB CA  1 ? 
ATOM   3628 C  C   . PRO   B 1 202 ? 30.586  29.637 51.453 1.000 23.423  ? 201 PRO   BBB C   1 ? 
ATOM   3629 O  O   . PRO   B 1 202 ? 29.748  30.466 51.156 1.000 23.133  ? 201 PRO   BBB O   1 ? 
ATOM   3630 C  CB  . PRO   B 1 202 ? 29.666  27.512 50.324 1.000 23.212  ? 201 PRO   BBB CB  1 ? 
ATOM   3631 C  CG  . PRO   B 1 202 ? 28.691  26.468 50.838 1.000 25.265  ? 201 PRO   BBB CG  1 ? 
ATOM   3632 C  CD  . PRO   B 1 202 ? 27.885  27.230 51.879 1.000 22.175  ? 201 PRO   BBB CD  1 ? 
ATOM   3633 N  N   . PRO   B 1 203 ? 31.909  29.899 51.510 1.000 20.662  ? 202 PRO   BBB N   1 ? 
ATOM   3634 C  CA  . PRO   B 1 203 ? 32.912  28.812 51.518 1.000 21.812  ? 202 PRO   BBB CA  1 ? 
ATOM   3635 C  C   . PRO   B 1 203 ? 33.344  28.248 52.888 1.000 21.293  ? 202 PRO   BBB C   1 ? 
ATOM   3636 O  O   . PRO   B 1 203 ? 34.312  27.426 52.925 1.000 23.396  ? 202 PRO   BBB O   1 ? 
ATOM   3637 C  CB  . PRO   B 1 203 ? 34.135  29.489 50.892 1.000 26.229  ? 202 PRO   BBB CB  1 ? 
ATOM   3638 C  CG  . PRO   B 1 203 ? 34.012  30.920 51.374 1.000 26.543  ? 202 PRO   BBB CG  1 ? 
ATOM   3639 C  CD  . PRO   B 1 203 ? 32.522  31.215 51.293 1.000 24.552  ? 202 PRO   BBB CD  1 ? 
ATOM   3640 N  N   . LEU   B 1 204 ? 32.563  28.497 53.946 1.000 24.293  ? 203 LEU   BBB N   1 ? 
ATOM   3641 C  CA  . LEU   B 1 204 ? 32.651  27.764 55.257 1.000 22.494  ? 203 LEU   BBB CA  1 ? 
ATOM   3642 C  C   . LEU   B 1 204 ? 34.017  27.948 55.937 1.000 22.403  ? 203 LEU   BBB C   1 ? 
ATOM   3643 O  O   . LEU   B 1 204 ? 34.343  27.169 56.841 1.000 22.808  ? 203 LEU   BBB O   1 ? 
ATOM   3644 C  CB  . LEU   B 1 204 ? 32.346  26.270 55.022 1.000 23.601  ? 203 LEU   BBB CB  1 ? 
ATOM   3645 C  CG  . LEU   B 1 204 ? 30.912  26.000 54.592 1.000 25.297  ? 203 LEU   BBB CG  1 ? 
ATOM   3646 C  CD1 . LEU   B 1 204 ? 30.759  24.549 54.117 1.000 32.157  ? 203 LEU   BBB CD1 1 ? 
ATOM   3647 C  CD2 . LEU   B 1 204 ? 29.961  26.282 55.744 1.000 24.002  ? 203 LEU   BBB CD2 1 ? 
ATOM   3648 N  N   . TYR   B 1 205 ? 34.776  28.969 55.560 1.000 22.882  ? 204 TYR   BBB N   1 ? 
ATOM   3649 C  CA  . TYR   B 1 205 ? 36.104  29.255 56.143 1.000 21.237  ? 204 TYR   BBB CA  1 ? 
ATOM   3650 C  C   . TYR   B 1 205 ? 35.972  29.275 57.662 1.000 19.211  ? 204 TYR   BBB C   1 ? 
ATOM   3651 O  O   . TYR   B 1 205 ? 34.993  29.812 58.221 1.000 23.716  ? 204 TYR   BBB O   1 ? 
ATOM   3652 C  CB  . TYR   B 1 205 ? 36.657  30.575 55.612 1.000 24.231  ? 204 TYR   BBB CB  1 ? 
ATOM   3653 C  CG  . TYR   B 1 205 ? 37.110  30.587 54.161 1.000 25.572  ? 204 TYR   BBB CG  1 ? 
ATOM   3654 C  CD1 . TYR   B 1 205 ? 37.880  29.555 53.631 1.000 33.824  ? 204 TYR   BBB CD1 1 ? 
ATOM   3655 C  CD2 . TYR   B 1 205 ? 36.824  31.648 53.317 1.000 32.251  ? 204 TYR   BBB CD2 1 ? 
ATOM   3656 C  CE1 . TYR   B 1 205 ? 38.325  29.574 52.313 1.000 37.777  ? 204 TYR   BBB CE1 1 ? 
ATOM   3657 C  CE2 . TYR   B 1 205 ? 37.257  31.680 51.996 1.000 34.010  ? 204 TYR   BBB CE2 1 ? 
ATOM   3658 C  CZ  . TYR   B 1 205 ? 38.024  30.641 51.481 1.000 42.073  ? 204 TYR   BBB CZ  1 ? 
ATOM   3659 O  OH  . TYR   B 1 205 ? 38.492  30.639 50.180 1.000 37.072  ? 204 TYR   BBB OH  1 ? 
ATOM   3660 N  N   . GLU   B 1 206 ? 36.968  28.723 58.333 1.000 21.755  ? 205 GLU   BBB N   1 ? 
ATOM   3661 C  CA  . GLU   B 1 206 ? 37.002  28.662 59.814 1.000 25.324  ? 205 GLU   BBB CA  1 ? 
ATOM   3662 C  C   . GLU   B 1 206 ? 37.737  29.907 60.321 1.000 25.125  ? 205 GLU   BBB C   1 ? 
ATOM   3663 O  O   . GLU   B 1 206 ? 38.802  29.790 60.914 1.000 26.453  ? 205 GLU   BBB O   1 ? 
ATOM   3664 C  CB  . GLU   B 1 206 ? 37.608  27.321 60.230 1.000 25.698  ? 205 GLU   BBB CB  1 ? 
ATOM   3665 C  CG  . GLU   B 1 206 ? 36.680  26.164 59.867 1.000 25.208  ? 205 GLU   BBB CG  1 ? 
ATOM   3666 C  CD  . GLU   B 1 206 ? 37.093  24.797 60.366 1.000 26.098  ? 205 GLU   BBB CD  1 ? 
ATOM   3667 O  OE1 . GLU   B 1 206 ? 36.210  23.948 60.480 1.000 24.895  ? 205 GLU   BBB OE1 1 ? 
ATOM   3668 O  OE2 . GLU   B 1 206 ? 38.287  24.603 60.619 1.000 30.245  ? 205 GLU   BBB OE2 1 ? 
ATOM   3669 N  N   . SER   B 1 207 ? 37.161  31.076 60.055 1.000 23.808  ? 206 SER   BBB N   1 ? 
ATOM   3670 C  CA  . SER   B 1 207 ? 37.831  32.399 60.165 1.000 21.868  ? 206 SER   BBB CA  1 ? 
ATOM   3671 C  C   . SER   B 1 207 ? 37.045  33.335 61.090 1.000 22.804  ? 206 SER   BBB C   1 ? 
ATOM   3672 O  O   . SER   B 1 207 ? 37.414  34.541 61.179 1.000 26.734  ? 206 SER   BBB O   1 ? 
ATOM   3673 C  CB  . SER   B 1 207 ? 37.971  33.016 58.802 1.000 24.505  ? 206 SER   BBB CB  1 ? 
ATOM   3674 O  OG  . SER   B 1 207 ? 36.719  33.013 58.133 1.000 25.869  ? 206 SER   BBB OG  1 ? 
ATOM   3675 N  N   . VAL   B 1 208 ? 36.019  32.813 61.746 1.000 20.995  ? 207 VAL   BBB N   1 ? 
ATOM   3676 C  CA  . VAL   B 1 208 ? 34.990  33.581 62.476 1.000 20.065  ? 207 VAL   BBB CA  1 ? 
ATOM   3677 C  C   . VAL   B 1 208 ? 35.114  33.451 63.985 1.000 21.854  ? 207 VAL   BBB C   1 ? 
ATOM   3678 O  O   . VAL   B 1 208 ? 35.062  32.335 64.521 1.000 22.790  ? 207 VAL   BBB O   1 ? 
ATOM   3679 C  CB  . VAL   B 1 208 ? 33.559  33.306 62.022 1.000 19.825  ? 207 VAL   BBB CB  1 ? 
ATOM   3680 C  CG1 . VAL   B 1 208 ? 32.596  34.222 62.780 1.000 19.459  ? 207 VAL   BBB CG1 1 ? 
ATOM   3681 C  CG2 . VAL   B 1 208 ? 33.430  33.541 60.534 1.000 21.737  ? 207 VAL   BBB CG2 1 ? 
ATOM   3682 N  N   . THR   B 1 209 ? 35.308  34.591 64.646 1.000 20.250  ? 208 THR   BBB N   1 ? 
ATOM   3683 C  CA  . THR   B 1 209 ? 35.079  34.717 66.099 1.000 19.620  ? 208 THR   BBB CA  1 ? 
ATOM   3684 C  C   . THR   B 1 209 ? 33.620  35.121 66.272 1.000 18.429  ? 208 THR   BBB C   1 ? 
ATOM   3685 O  O   . THR   B 1 209 ? 33.255  36.266 65.937 1.000 21.216  ? 208 THR   BBB O   1 ? 
ATOM   3686 C  CB  . THR   B 1 209 ? 36.029  35.707 66.780 1.000 20.747  ? 208 THR   BBB CB  1 ? 
ATOM   3687 O  OG1 . THR   B 1 209 ? 37.389  35.330 66.554 1.000 21.954  ? 208 THR   BBB OG1 1 ? 
ATOM   3688 C  CG2 . THR   B 1 209 ? 35.809  35.799 68.273 1.000 24.103  ? 208 THR   BBB CG2 1 ? 
ATOM   3689 N  N   . TRP   B 1 210 ? 32.785  34.210 66.723 1.000 20.450  ? 209 TRP   BBB N   1 ? 
ATOM   3690 C  CA  . TRP   B 1 210 ? 31.341  34.447 66.947 1.000 18.237  ? 209 TRP   BBB CA  1 ? 
ATOM   3691 C  C   . TRP   B 1 210 ? 31.112  35.148 68.283 1.000 18.731  ? 209 TRP   BBB C   1 ? 
ATOM   3692 O  O   . TRP   B 1 210 ? 31.699  34.742 69.311 1.000 20.378  ? 209 TRP   BBB O   1 ? 
ATOM   3693 C  CB  . TRP   B 1 210 ? 30.521  33.145 66.903 1.000 18.296  ? 209 TRP   BBB CB  1 ? 
ATOM   3694 C  CG  . TRP   B 1 210 ? 30.308  32.708 65.499 1.000 16.883  ? 209 TRP   BBB CG  1 ? 
ATOM   3695 C  CD1 . TRP   B 1 210 ? 31.070  31.841 64.768 1.000 19.300  ? 209 TRP   BBB CD1 1 ? 
ATOM   3696 C  CD2 . TRP   B 1 210 ? 29.301  33.203 64.621 1.000 16.709  ? 209 TRP   BBB CD2 1 ? 
ATOM   3697 N  NE1 . TRP   B 1 210 ? 30.597  31.763 63.488 1.000 19.708  ? 209 TRP   BBB NE1 1 ? 
ATOM   3698 C  CE2 . TRP   B 1 210 ? 29.502  32.601 63.371 1.000 18.733  ? 209 TRP   BBB CE2 1 ? 
ATOM   3699 C  CE3 . TRP   B 1 210 ? 28.214  34.052 64.794 1.000 16.901  ? 209 TRP   BBB CE3 1 ? 
ATOM   3700 C  CZ2 . TRP   B 1 210 ? 28.689  32.896 62.275 1.000 19.509  ? 209 TRP   BBB CZ2 1 ? 
ATOM   3701 C  CZ3 . TRP   B 1 210 ? 27.404  34.330 63.720 1.000 19.905  ? 209 TRP   BBB CZ3 1 ? 
ATOM   3702 C  CH2 . TRP   B 1 210 ? 27.612  33.733 62.482 1.000 19.006  ? 209 TRP   BBB CH2 1 ? 
ATOM   3703 N  N   . ILE   B 1 211 ? 30.217  36.165 68.238 1.000 18.988  ? 210 ILE   BBB N   1 ? 
ATOM   3704 C  CA  . ILE   B 1 211 ? 29.676  36.847 69.436 1.000 20.272  ? 210 ILE   BBB CA  1 ? 
ATOM   3705 C  C   . ILE   B 1 211 ? 28.168  36.661 69.435 1.000 19.575  ? 210 ILE   BBB C   1 ? 
ATOM   3706 O  O   . ILE   B 1 211 ? 27.505  37.245 68.540 1.000 22.024  ? 210 ILE   BBB O   1 ? 
ATOM   3707 C  CB  . ILE   B 1 211 ? 29.994  38.361 69.304 1.000 20.479  ? 210 ILE   BBB CB  1 ? 
ATOM   3708 C  CG1 . ILE   B 1 211 ? 31.484  38.670 69.149 1.000 22.035  ? 210 ILE   BBB CG1 1 ? 
ATOM   3709 C  CG2 . ILE   B 1 211 ? 29.363  39.054 70.487 1.000 22.036  ? 210 ILE   BBB CG2 1 ? 
ATOM   3710 C  CD1 . ILE   B 1 211 ? 32.334  38.260 70.292 1.000 25.425  ? 210 ILE   BBB CD1 1 ? 
ATOM   3711 N  N   . ILE   B 1 212 ? 27.658  35.704 70.230 1.000 19.311  ? 211 ILE   BBB N   1 ? 
ATOM   3712 C  CA  . ILE   B 1 212 ? 26.209  35.408 70.281 1.000 18.962  ? 211 ILE   BBB CA  1 ? 
ATOM   3713 C  C   . ILE   B 1 212 ? 25.586  36.127 71.466 1.000 16.389  ? 211 ILE   BBB C   1 ? 
ATOM   3714 O  O   . ILE   B 1 212 ? 25.994  35.934 72.615 1.000 19.026  ? 211 ILE   BBB O   1 ? 
ATOM   3715 C  CB  . ILE   B 1 212 ? 25.965  33.885 70.354 1.000 20.039  ? 211 ILE   BBB CB  1 ? 
ATOM   3716 C  CG1 . ILE   B 1 212 ? 26.790  33.229 69.247 1.000 19.732  ? 211 ILE   BBB CG1 1 ? 
ATOM   3717 C  CG2 . ILE   B 1 212 ? 24.465  33.682 70.271 1.000 20.059  ? 211 ILE   BBB CG2 1 ? 
ATOM   3718 C  CD1 . ILE   B 1 212 ? 26.376  33.498 67.817 1.000 19.188  ? 211 ILE   BBB CD1 1 ? 
ATOM   3719 N  N   . CYS   B 1 213 ? 24.680  37.063 71.142 1.000 21.237  ? 212 CYS   BBB N   1 ? 
ATOM   3720 C  CA  . CYS   B 1 213 ? 24.018  37.836 72.207 1.000 20.008  ? 212 CYS   BBB CA  1 ? 
ATOM   3721 C  C   . CYS   B 1 213 ? 23.175  36.912 73.091 1.000 17.820  ? 212 CYS   BBB C   1 ? 
ATOM   3722 O  O   . CYS   B 1 213 ? 22.435  36.092 72.536 1.000 18.043  ? 212 CYS   BBB O   1 ? 
ATOM   3723 C  CB  . CYS   B 1 213 ? 23.163  38.943 71.591 1.000 20.234  ? 212 CYS   BBB CB  1 ? 
ATOM   3724 S  SG  . CYS   B 1 213 ? 24.151  40.308 70.907 1.000 23.650  ? 212 CYS   BBB SG  1 ? 
ATOM   3725 N  N   . LYS   B 1 214 ? 23.258  37.074 74.405 1.000 18.487  ? 213 LYS   BBB N   1 ? 
ATOM   3726 C  CA  . LYS   B 1 214 ? 22.378  36.389 75.370 1.000 18.380  ? 213 LYS   BBB CA  1 ? 
ATOM   3727 C  C   . LYS   B 1 214 ? 20.923  36.771 75.130 1.000 18.415  ? 213 LYS   BBB C   1 ? 
ATOM   3728 O  O   . LYS   B 1 214 ? 20.028  35.959 75.292 1.000 21.875  ? 213 LYS   BBB O   1 ? 
ATOM   3729 C  CB  . LYS   B 1 214 ? 22.823  36.711 76.791 1.000 23.986  ? 213 LYS   BBB CB  1 ? 
ATOM   3730 C  CG  . LYS   B 1 214 ? 22.031  36.012 77.895 1.000 27.300  ? 213 LYS   BBB CG  1 ? 
ATOM   3731 C  CD  . LYS   B 1 214 ? 22.244  36.576 79.303 1.000 35.029  ? 213 LYS   BBB CD  1 ? 
ATOM   3732 C  CE  . LYS   B 1 214 ? 21.842  38.034 79.376 1.000 41.115  ? 213 LYS   BBB CE  1 ? 
ATOM   3733 N  NZ  . LYS   B 1 214 ? 21.991  38.634 80.721 1.000 50.224  ? 213 LYS   BBB NZ  1 ? 
ATOM   3734 N  N   . GLU   B 1 215 ? 20.648  38.036 74.857 1.000 19.222  ? 214 GLU   BBB N   1 ? 
ATOM   3735 C  CA  . GLU   B 1 215 ? 19.262  38.531 74.686 1.000 19.479  ? 214 GLU   BBB CA  1 ? 
ATOM   3736 C  C   . GLU   B 1 215 ? 18.840  38.412 73.217 1.000 18.215  ? 214 GLU   BBB C   1 ? 
ATOM   3737 O  O   . GLU   B 1 215 ? 19.648  38.690 72.286 1.000 20.015  ? 214 GLU   BBB O   1 ? 
ATOM   3738 C  CB  . GLU   B 1 215 ? 19.163  39.985 75.142 1.000 22.775  ? 214 GLU   BBB CB  1 ? 
ATOM   3739 C  CG  . GLU   B 1 215 ? 19.597  40.176 76.583 1.000 26.937  ? 214 GLU   BBB CG  1 ? 
ATOM   3740 C  CD  . GLU   B 1 215 ? 18.921  39.379 77.702 1.000 38.122  ? 214 GLU   BBB CD  1 ? 
ATOM   3741 O  OE1 . GLU   B 1 215 ? 17.745  38.949 77.546 1.000 42.424  ? 214 GLU   BBB OE1 1 ? 
ATOM   3742 O  OE2 . GLU   B 1 215 ? 19.565  39.208 78.767 1.000 46.275  ? 214 GLU   BBB OE2 1 ? 
ATOM   3743 N  N   . SER   B 1 216 ? 17.590  38.027 73.022 1.000 20.821  ? 215 SER   BBB N   1 ? 
ATOM   3744 C  CA  . SER   B 1 216 ? 16.933  37.940 71.710 1.000 21.005  ? 215 SER   BBB CA  1 ? 
ATOM   3745 C  C   . SER   B 1 216 ? 16.261  39.299 71.399 1.000 19.069  ? 215 SER   BBB C   1 ? 
ATOM   3746 O  O   . SER   B 1 216 ? 16.076  40.109 72.363 1.000 21.922  ? 215 SER   BBB O   1 ? 
ATOM   3747 C  CB  . SER   B 1 216 ? 15.951  36.802 71.686 1.000 19.760  ? 215 SER   BBB CB  1 ? 
ATOM   3748 O  OG  . SER   B 1 216 ? 14.932  36.958 72.656 1.000 23.782  ? 215 SER   BBB OG  1 ? 
ATOM   3749 N  N   . ILE   B 1 217 ? 15.859  39.437 70.145 1.000 19.771  ? 216 ILE   BBB N   1 ? 
ATOM   3750 C  CA  . ILE   B 1 217 ? 15.001  40.559 69.658 1.000 18.012  ? 216 ILE   BBB CA  1 ? 
ATOM   3751 C  C   . ILE   B 1 217 ? 13.752  39.925 69.058 1.000 19.057  ? 216 ILE   BBB C   1 ? 
ATOM   3752 O  O   . ILE   B 1 217 ? 13.739  38.661 68.841 1.000 20.515  ? 216 ILE   BBB O   1 ? 
ATOM   3753 C  CB  . ILE   B 1 217 ? 15.722  41.433 68.624 1.000 20.427  ? 216 ILE   BBB CB  1 ? 
ATOM   3754 C  CG1 . ILE   B 1 217 ? 16.122  40.637 67.381 1.000 19.712  ? 216 ILE   BBB CG1 1 ? 
ATOM   3755 C  CG2 . ILE   B 1 217 ? 16.889  42.182 69.261 1.000 19.935  ? 216 ILE   BBB CG2 1 ? 
ATOM   3756 C  CD1 . ILE   B 1 217 ? 16.661  41.470 66.249 1.000 18.677  ? 216 ILE   BBB CD1 1 ? 
ATOM   3757 N  N   . SER   B 1 218 ? 12.700  40.690 68.917 1.000 21.094  ? 217 SER   BBB N   1 ? 
ATOM   3758 C  CA  A SER   B 1 218 ? 11.403  40.227 68.371 0.500 20.503  ? 217 SER   BBB CA  1 ? 
ATOM   3759 C  CA  B SER   B 1 218 ? 11.383  40.283 68.369 0.500 20.380  ? 217 SER   BBB CA  1 ? 
ATOM   3760 C  C   . SER   B 1 218 ? 11.361  40.297 66.837 1.000 18.030  ? 217 SER   BBB C   1 ? 
ATOM   3761 O  O   . SER   B 1 218 ? 12.225  40.882 66.197 1.000 19.669  ? 217 SER   BBB O   1 ? 
ATOM   3762 C  CB  A SER   B 1 218 ? 10.243  40.970 69.011 0.500 21.163  ? 217 SER   BBB CB  1 ? 
ATOM   3763 C  CB  B SER   B 1 218 ? 10.277  41.167 68.914 0.500 21.751  ? 217 SER   BBB CB  1 ? 
ATOM   3764 O  OG  A SER   B 1 218 ? 9.940   42.174 68.329 0.500 23.107  ? 217 SER   BBB OG  1 ? 
ATOM   3765 O  OG  B SER   B 1 218 ? 9.023   40.492 68.869 0.500 24.370  ? 217 SER   BBB OG  1 ? 
ATOM   3766 N  N   . VAL   B 1 219 ? 10.384  39.581 66.278 1.000 18.643  ? 218 VAL   BBB N   1 ? 
ATOM   3767 C  CA  . VAL   B 1 219 ? 10.021  39.584 64.842 1.000 18.714  ? 218 VAL   BBB CA  1 ? 
ATOM   3768 C  C   . VAL   B 1 219 ? 8.612   39.011 64.769 1.000 20.183  ? 218 VAL   BBB C   1 ? 
ATOM   3769 O  O   . VAL   B 1 219 ? 8.279   38.188 65.634 1.000 20.638  ? 218 VAL   BBB O   1 ? 
ATOM   3770 C  CB  . VAL   B 1 219 ? 11.035  38.839 63.970 1.000 18.704  ? 218 VAL   BBB CB  1 ? 
ATOM   3771 C  CG1 . VAL   B 1 219 ? 11.036  37.343 64.247 1.000 21.949  ? 218 VAL   BBB CG1 1 ? 
ATOM   3772 C  CG2 . VAL   B 1 219 ? 10.789  39.082 62.500 1.000 19.149  ? 218 VAL   BBB CG2 1 ? 
ATOM   3773 N  N   . SER   B 1 220 ? 7.741   39.580 63.946 1.000 19.370  ? 219 SER   BBB N   1 ? 
ATOM   3774 C  CA  . SER   B 1 220 ? 6.364   39.075 63.816 1.000 21.335  ? 219 SER   BBB CA  1 ? 
ATOM   3775 C  C   . SER   B 1 220 ? 6.357   37.961 62.767 1.000 18.711  ? 219 SER   BBB C   1 ? 
ATOM   3776 O  O   . SER   B 1 220 ? 7.247   37.895 61.874 1.000 18.856  ? 219 SER   BBB O   1 ? 
ATOM   3777 C  CB  . SER   B 1 220 ? 5.381   40.158 63.488 1.000 22.266  ? 219 SER   BBB CB  1 ? 
ATOM   3778 O  OG  . SER   B 1 220 ? 5.518   40.555 62.146 1.000 23.537  ? 219 SER   BBB OG  1 ? 
ATOM   3779 N  N   . SER   B 1 221 ? 5.304   37.157 62.822 1.000 21.782  ? 220 SER   BBB N   1 ? 
ATOM   3780 C  CA  . SER   B 1 221 ? 5.006   36.146 61.785 1.000 21.927  ? 220 SER   BBB CA  1 ? 
ATOM   3781 C  C   . SER   B 1 221 ? 4.970   36.796 60.393 1.000 22.451  ? 220 SER   BBB C   1 ? 
ATOM   3782 O  O   . SER   B 1 221 ? 5.481   36.176 59.444 1.000 20.269  ? 220 SER   BBB O   1 ? 
ATOM   3783 C  CB  . SER   B 1 221 ? 3.744   35.395 62.118 1.000 28.087  ? 220 SER   BBB CB  1 ? 
ATOM   3784 O  OG  . SER   B 1 221 ? 3.576   34.336 61.186 1.000 30.515  ? 220 SER   BBB OG  1 ? 
ATOM   3785 N  N   . GLU   B 1 222 ? 4.414   38.015 60.249 1.000 22.101  ? 221 GLU   BBB N   1 ? 
ATOM   3786 C  CA  . GLU   B 1 222 ? 4.237   38.637 58.912 1.000 20.713  ? 221 GLU   BBB CA  1 ? 
ATOM   3787 C  C   . GLU   B 1 222 ? 5.592   39.200 58.442 1.000 18.913  ? 221 GLU   BBB C   1 ? 
ATOM   3788 O  O   . GLU   B 1 222 ? 5.868   39.230 57.208 1.000 19.740  ? 221 GLU   BBB O   1 ? 
ATOM   3789 C  CB  . GLU   B 1 222 ? 3.134   39.705 58.954 1.000 22.729  ? 221 GLU   BBB CB  1 ? 
ATOM   3790 C  CG  . GLU   B 1 222 ? 1.766   39.129 59.274 1.000 25.445  ? 221 GLU   BBB CG  1 ? 
ATOM   3791 C  CD  . GLU   B 1 222 ? 1.568   38.566 60.677 1.000 24.529  ? 221 GLU   BBB CD  1 ? 
ATOM   3792 O  OE1 . GLU   B 1 222 ? 2.083   39.157 61.645 1.000 28.561  ? 221 GLU   BBB OE1 1 ? 
ATOM   3793 O  OE2 . GLU   B 1 222 ? 0.818   37.591 60.806 1.000 28.170  ? 221 GLU   BBB OE2 1 ? 
ATOM   3794 N  N   . GLN   B 1 223 ? 6.437   39.627 59.370 1.000 19.510  ? 222 GLN   BBB N   1 ? 
ATOM   3795 C  CA  . GLN   B 1 223 ? 7.793   40.105 59.002 1.000 19.477  ? 222 GLN   BBB CA  1 ? 
ATOM   3796 C  C   . GLN   B 1 223 ? 8.606   38.916 58.481 1.000 18.812  ? 222 GLN   BBB C   1 ? 
ATOM   3797 O  O   . GLN   B 1 223 ? 9.272   39.047 57.473 1.000 18.456  ? 222 GLN   BBB O   1 ? 
ATOM   3798 C  CB  . GLN   B 1 223 ? 8.430   40.769 60.204 1.000 18.668  ? 222 GLN   BBB CB  1 ? 
ATOM   3799 C  CG  . GLN   B 1 223 ? 7.816   42.127 60.522 1.000 20.510  ? 222 GLN   BBB CG  1 ? 
ATOM   3800 C  CD  . GLN   B 1 223 ? 8.480   42.784 61.699 1.000 20.773  ? 222 GLN   BBB CD  1 ? 
ATOM   3801 O  OE1 . GLN   B 1 223 ? 8.764   42.214 62.743 1.000 21.662  ? 222 GLN   BBB OE1 1 ? 
ATOM   3802 N  NE2 . GLN   B 1 223 ? 8.660   44.112 61.565 1.000 22.201  ? 222 GLN   BBB NE2 1 ? 
ATOM   3803 N  N   . LEU   B 1 224 ? 8.503   37.762 59.123 1.000 19.454  ? 223 LEU   BBB N   1 ? 
ATOM   3804 C  CA  . LEU   B 1 224 ? 9.200   36.575 58.565 1.000 20.913  ? 223 LEU   BBB CA  1 ? 
ATOM   3805 C  C   . LEU   B 1 224 ? 8.629   36.237 57.172 1.000 19.077  ? 223 LEU   BBB C   1 ? 
ATOM   3806 O  O   . LEU   B 1 224 ? 9.413   35.850 56.276 1.000 21.361  ? 223 LEU   BBB O   1 ? 
ATOM   3807 C  CB  . LEU   B 1 224 ? 9.059   35.408 59.543 1.000 19.470  ? 223 LEU   BBB CB  1 ? 
ATOM   3808 C  CG  . LEU   B 1 224 ? 9.761   35.593 60.886 1.000 22.446  ? 223 LEU   BBB CG  1 ? 
ATOM   3809 C  CD1 . LEU   B 1 224 ? 9.340   34.506 61.877 1.000 26.379  ? 223 LEU   BBB CD1 1 ? 
ATOM   3810 C  CD2 . LEU   B 1 224 ? 11.277  35.601 60.729 1.000 27.043  ? 223 LEU   BBB CD2 1 ? 
ATOM   3811 N  N   . ALA   B 1 225 ? 7.311   36.343 56.972 1.000 18.555  ? 224 ALA   BBB N   1 ? 
ATOM   3812 C  CA  . ALA   B 1 225 ? 6.702   36.074 55.652 1.000 19.980  ? 224 ALA   BBB CA  1 ? 
ATOM   3813 C  C   . ALA   B 1 225 ? 7.324   37.003 54.593 1.000 20.617  ? 224 ALA   BBB C   1 ? 
ATOM   3814 O  O   . ALA   B 1 225 ? 7.512   36.558 53.444 1.000 22.071  ? 224 ALA   BBB O   1 ? 
ATOM   3815 C  CB  . ALA   B 1 225 ? 5.207   36.153 55.727 1.000 22.554  ? 224 ALA   BBB CB  1 ? 
ATOM   3816 N  N   . GLN   B 1 226 ? 7.643   38.258 54.940 1.000 21.013  ? 225 GLN   BBB N   1 ? 
ATOM   3817 C  CA  . GLN   B 1 226 ? 8.301   39.156 53.963 1.000 23.414  ? 225 GLN   BBB CA  1 ? 
ATOM   3818 C  C   . GLN   B 1 226 ? 9.656   38.598 53.546 1.000 20.799  ? 225 GLN   BBB C   1 ? 
ATOM   3819 O  O   . GLN   B 1 226 ? 9.945   38.668 52.360 1.000 20.713  ? 225 GLN   BBB O   1 ? 
ATOM   3820 C  CB  . GLN   B 1 226 ? 8.450   40.565 54.520 1.000 23.920  ? 225 GLN   BBB CB  1 ? 
ATOM   3821 C  CG  . GLN   B 1 226 ? 7.138   41.294 54.596 1.000 24.592  ? 225 GLN   BBB CG  1 ? 
ATOM   3822 C  CD  . GLN   B 1 226 ? 7.361   42.750 54.949 1.000 24.016  ? 225 GLN   BBB CD  1 ? 
ATOM   3823 O  OE1 . GLN   B 1 226 ? 7.168   43.131 56.105 1.000 27.800  ? 225 GLN   BBB OE1 1 ? 
ATOM   3824 N  NE2 . GLN   B 1 226 ? 7.810   43.559 53.987 1.000 26.061  ? 225 GLN   BBB NE2 1 ? 
ATOM   3825 N  N   . PHE   B 1 227 ? 10.466  38.077 54.467 1.000 18.788  ? 226 PHE   BBB N   1 ? 
ATOM   3826 C  CA  . PHE   B 1 227 ? 11.769  37.472 54.091 1.000 21.142  ? 226 PHE   BBB CA  1 ? 
ATOM   3827 C  C   . PHE   B 1 227 ? 11.501  36.321 53.117 1.000 18.763  ? 226 PHE   BBB C   1 ? 
ATOM   3828 O  O   . PHE   B 1 227 ? 12.195  36.176 52.082 1.000 20.505  ? 226 PHE   BBB O   1 ? 
ATOM   3829 C  CB  . PHE   B 1 227 ? 12.490  36.916 55.307 1.000 19.681  ? 226 PHE   BBB CB  1 ? 
ATOM   3830 C  CG  . PHE   B 1 227 ? 13.050  37.887 56.311 1.000 20.180  ? 226 PHE   BBB CG  1 ? 
ATOM   3831 C  CD1 . PHE   B 1 227 ? 13.289  39.234 56.019 1.000 24.344  ? 226 PHE   BBB CD1 1 ? 
ATOM   3832 C  CD2 . PHE   B 1 227 ? 13.353  37.437 57.585 1.000 25.782  ? 226 PHE   BBB CD2 1 ? 
ATOM   3833 C  CE1 . PHE   B 1 227 ? 13.825  40.065 56.982 1.000 28.115  ? 226 PHE   BBB CE1 1 ? 
ATOM   3834 C  CE2 . PHE   B 1 227 ? 13.891  38.285 58.544 1.000 26.558  ? 226 PHE   BBB CE2 1 ? 
ATOM   3835 C  CZ  . PHE   B 1 227 ? 14.133  39.588 58.231 1.000 27.203  ? 226 PHE   BBB CZ  1 ? 
ATOM   3836 N  N   . ARG   B 1 228 ? 10.473  35.529 53.421 1.000 20.179  ? 227 ARG   BBB N   1 ? 
ATOM   3837 C  CA  . ARG   B 1 228 ? 10.197  34.309 52.616 1.000 21.291  ? 227 ARG   BBB CA  1 ? 
ATOM   3838 C  C   . ARG   B 1 228 ? 9.585   34.674 51.263 1.000 20.612  ? 227 ARG   BBB C   1 ? 
ATOM   3839 O  O   . ARG   B 1 228 ? 9.484   33.792 50.396 1.000 26.270  ? 227 ARG   BBB O   1 ? 
ATOM   3840 C  CB  . ARG   B 1 228 ? 9.272   33.355 53.374 1.000 21.548  ? 227 ARG   BBB CB  1 ? 
ATOM   3841 C  CG  . ARG   B 1 228 ? 9.911   32.720 54.599 1.000 23.201  ? 227 ARG   BBB CG  1 ? 
ATOM   3842 C  CD  . ARG   B 1 228 ? 9.113   31.489 54.999 1.000 24.259  ? 227 ARG   BBB CD  1 ? 
ATOM   3843 N  NE  . ARG   B 1 228 ? 9.346   31.231 56.411 1.000 27.833  ? 227 ARG   BBB NE  1 ? 
ATOM   3844 C  CZ  . ARG   B 1 228 ? 8.595   31.676 57.408 1.000 28.516  ? 227 ARG   BBB CZ  1 ? 
ATOM   3845 N  NH1 . ARG   B 1 228 ? 8.963   31.413 58.660 1.000 33.623  ? 227 ARG   BBB NH1 1 ? 
ATOM   3846 N  NH2 . ARG   B 1 228 ? 7.496   32.389 57.161 1.000 27.659  ? 227 ARG   BBB NH2 1 ? 
ATOM   3847 N  N   . SER   B 1 229 ? 9.088   35.907 51.106 1.000 18.521  ? 228 SER   BBB N   1 ? 
ATOM   3848 C  CA  . SER   B 1 229 ? 8.485   36.350 49.828 1.000 21.474  ? 228 SER   BBB CA  1 ? 
ATOM   3849 C  C   . SER   B 1 229 ? 9.611   36.825 48.884 1.000 19.759  ? 228 SER   BBB C   1 ? 
ATOM   3850 O  O   . SER   B 1 229 ? 9.313   37.111 47.701 1.000 23.891  ? 228 SER   BBB O   1 ? 
ATOM   3851 C  CB  . SER   B 1 229 ? 7.421   37.426 50.063 1.000 27.757  ? 228 SER   BBB CB  1 ? 
ATOM   3852 O  OG  . SER   B 1 229 ? 8.030   38.672 50.386 1.000 37.983  ? 228 SER   BBB OG  1 ? 
ATOM   3853 N  N   . LEU   B 1 230 ? 10.867  36.934 49.357 1.000 19.446  ? 229 LEU   BBB N   1 ? 
ATOM   3854 C  CA  . LEU   B 1 230 ? 11.987  37.149 48.400 1.000 19.975  ? 229 LEU   BBB CA  1 ? 
ATOM   3855 C  C   . LEU   B 1 230 ? 12.117  35.919 47.494 1.000 18.642  ? 229 LEU   BBB C   1 ? 
ATOM   3856 O  O   . LEU   B 1 230 ? 11.784  34.824 47.943 1.000 24.645  ? 229 LEU   BBB O   1 ? 
ATOM   3857 C  CB  . LEU   B 1 230 ? 13.301  37.361 49.135 1.000 20.808  ? 229 LEU   BBB CB  1 ? 
ATOM   3858 C  CG  . LEU   B 1 230 ? 13.453  38.717 49.788 1.000 25.754  ? 229 LEU   BBB CG  1 ? 
ATOM   3859 C  CD1 . LEU   B 1 230 ? 14.670  38.682 50.683 1.000 28.582  ? 229 LEU   BBB CD1 1 ? 
ATOM   3860 C  CD2 . LEU   B 1 230 ? 13.522  39.838 48.737 1.000 28.347  ? 229 LEU   BBB CD2 1 ? 
ATOM   3861 N  N   . LEU   B 1 231 ? 12.599  36.121 46.280 1.000 19.020  ? 230 LEU   BBB N   1 ? 
ATOM   3862 C  CA  . LEU   B 1 231 ? 12.645  35.097 45.221 1.000 21.378  ? 230 LEU   BBB CA  1 ? 
ATOM   3863 C  C   . LEU   B 1 231 ? 14.110  34.755 44.942 1.000 23.111  ? 230 LEU   BBB C   1 ? 
ATOM   3864 O  O   . LEU   B 1 231 ? 14.948  35.682 44.856 1.000 20.029  ? 230 LEU   BBB O   1 ? 
ATOM   3865 C  CB  . LEU   B 1 231 ? 11.942  35.643 43.984 1.000 20.668  ? 230 LEU   BBB CB  1 ? 
ATOM   3866 C  CG  . LEU   B 1 231 ? 10.466  36.004 44.127 1.000 21.907  ? 230 LEU   BBB CG  1 ? 
ATOM   3867 C  CD1 . LEU   B 1 231 ? 9.911   36.369 42.760 1.000 28.023  ? 230 LEU   BBB CD1 1 ? 
ATOM   3868 C  CD2 . LEU   B 1 231 ? 9.616   34.900 44.738 1.000 24.569  ? 230 LEU   BBB CD2 1 ? 
ATOM   3869 N  N   . SER   B 1 232 ? 14.421  33.456 44.851 1.000 23.364  ? 231 SER   BBB N   1 ? 
ATOM   3870 C  CA  . SER   B 1 232 ? 15.789  32.940 44.605 1.000 21.847  ? 231 SER   BBB CA  1 ? 
ATOM   3871 C  C   . SER   B 1 232 ? 16.127  32.930 43.106 1.000 19.611  ? 231 SER   BBB C   1 ? 
ATOM   3872 O  O   . SER   B 1 232 ? 17.324  32.767 42.755 1.000 23.388  ? 231 SER   BBB O   1 ? 
ATOM   3873 C  CB  . SER   B 1 232 ? 15.952  31.557 45.199 1.000 22.082  ? 231 SER   BBB CB  1 ? 
ATOM   3874 O  OG  . SER   B 1 232 ? 15.002  30.683 44.615 1.000 26.715  ? 231 SER   BBB OG  1 ? 
ATOM   3875 N  N   . ASN   B 1 233 ? 15.118  33.004 42.251 1.000 20.030  ? 232 ASN   BBB N   1 ? 
ATOM   3876 C  CA  . ASN   B 1 233 ? 15.253  32.951 40.772 1.000 23.290  ? 232 ASN   BBB CA  1 ? 
ATOM   3877 C  C   . ASN   B 1 233 ? 15.639  34.341 40.252 1.000 22.160  ? 232 ASN   BBB C   1 ? 
ATOM   3878 O  O   . ASN   B 1 233 ? 15.427  35.338 40.987 1.000 22.447  ? 232 ASN   BBB O   1 ? 
ATOM   3879 C  CB  . ASN   B 1 233 ? 13.947  32.503 40.112 1.000 23.139  ? 232 ASN   BBB CB  1 ? 
ATOM   3880 C  CG  . ASN   B 1 233 ? 12.795  33.447 40.439 1.000 21.891  ? 232 ASN   BBB CG  1 ? 
ATOM   3881 O  OD1 . ASN   B 1 233 ? 12.227  33.383 41.526 1.000 24.135  ? 232 ASN   BBB OD1 1 ? 
ATOM   3882 N  ND2 . ASN   B 1 233 ? 12.451  34.333 39.523 1.000 20.712  ? 232 ASN   BBB ND2 1 ? 
ATOM   3883 N  N   . VAL   B 1 234 ? 16.137  34.388 39.026 1.000 23.806  ? 233 VAL   BBB N   1 ? 
ATOM   3884 C  CA  . VAL   B 1 234 ? 16.384  35.659 38.291 1.000 21.532  ? 233 VAL   BBB CA  1 ? 
ATOM   3885 C  C   . VAL   B 1 234 ? 15.050  36.143 37.704 1.000 25.530  ? 233 VAL   BBB C   1 ? 
ATOM   3886 O  O   . VAL   B 1 234 ? 14.109  35.319 37.453 1.000 26.194  ? 233 VAL   BBB O   1 ? 
ATOM   3887 C  CB  . VAL   B 1 234 ? 17.477  35.520 37.220 1.000 29.387  ? 233 VAL   BBB CB  1 ? 
ATOM   3888 C  CG1 . VAL   B 1 234 ? 18.788  35.039 37.837 1.000 29.096  ? 233 VAL   BBB CG1 1 ? 
ATOM   3889 C  CG2 . VAL   B 1 234 ? 17.030  34.604 36.089 1.000 30.869  ? 233 VAL   BBB CG2 1 ? 
ATOM   3890 N  N   . GLU   B 1 235 ? 14.972  37.448 37.482 1.000 26.466  ? 234 GLU   BBB N   1 ? 
ATOM   3891 C  CA  . GLU   B 1 235 ? 13.791  38.117 36.882 1.000 25.761  ? 234 GLU   BBB CA  1 ? 
ATOM   3892 C  C   . GLU   B 1 235 ? 13.404  37.375 35.608 1.000 25.145  ? 234 GLU   BBB C   1 ? 
ATOM   3893 O  O   . GLU   B 1 235 ? 14.312  36.988 34.841 1.000 30.123  ? 234 GLU   BBB O   1 ? 
ATOM   3894 C  CB  . GLU   B 1 235 ? 14.113  39.564 36.522 1.000 27.607  ? 234 GLU   BBB CB  1 ? 
ATOM   3895 C  CG  . GLU   B 1 235 ? 12.886  40.400 36.180 1.000 29.865  ? 234 GLU   BBB CG  1 ? 
ATOM   3896 C  CD  . GLU   B 1 235 ? 13.171  41.893 36.079 1.000 34.581  ? 234 GLU   BBB CD  1 ? 
ATOM   3897 O  OE1 . GLU   B 1 235 ? 13.325  42.547 37.127 1.000 36.891  ? 234 GLU   BBB OE1 1 ? 
ATOM   3898 O  OE2 . GLU   B 1 235 ? 13.243  42.397 34.962 1.000 42.242  ? 234 GLU   BBB OE2 1 ? 
ATOM   3899 N  N   . GLY   B 1 236 ? 12.111  37.197 35.396 1.000 25.085  ? 235 GLY   BBB N   1 ? 
ATOM   3900 C  CA  . GLY   B 1 236 ? 11.574  36.540 34.189 1.000 31.653  ? 235 GLY   BBB CA  1 ? 
ATOM   3901 C  C   . GLY   B 1 236 ? 11.318  35.055 34.398 1.000 28.380  ? 235 GLY   BBB C   1 ? 
ATOM   3902 O  O   . GLY   B 1 236 ? 10.383  34.526 33.753 1.000 38.454  ? 235 GLY   BBB O   1 ? 
ATOM   3903 N  N   . ASP   B 1 237 ? 12.089  34.391 35.253 1.000 25.086  ? 236 ASP   BBB N   1 ? 
ATOM   3904 C  CA  . ASP   B 1 237 ? 11.894  32.933 35.504 1.000 28.584  ? 236 ASP   BBB CA  1 ? 
ATOM   3905 C  C   . ASP   B 1 237 ? 10.718  32.731 36.453 1.000 25.455  ? 236 ASP   BBB C   1 ? 
ATOM   3906 O  O   . ASP   B 1 237 ? 10.257  33.718 37.078 1.000 31.691  ? 236 ASP   BBB O   1 ? 
ATOM   3907 C  CB  . ASP   B 1 237 ? 13.165  32.266 36.025 1.000 28.704  ? 236 ASP   BBB CB  1 ? 
ATOM   3908 C  CG  . ASP   B 1 237 ? 14.234  32.105 34.956 1.000 29.911  ? 236 ASP   BBB CG  1 ? 
ATOM   3909 O  OD1 . ASP   B 1 237 ? 13.925  32.347 33.776 1.000 36.042  ? 236 ASP   BBB OD1 1 ? 
ATOM   3910 O  OD2 . ASP   B 1 237 ? 15.370  31.773 35.322 1.000 33.442  ? 236 ASP   BBB OD2 1 ? 
ATOM   3911 N  N   . ASN   B 1 238 ? 10.227  31.495 36.559 1.000 26.570  ? 237 ASN   BBB N   1 ? 
ATOM   3912 C  CA  . ASN   B 1 238 ? 9.112   31.233 37.489 1.000 28.110  ? 237 ASN   BBB CA  1 ? 
ATOM   3913 C  C   . ASN   B 1 238 ? 9.593   31.559 38.904 1.000 25.970  ? 237 ASN   BBB C   1 ? 
ATOM   3914 O  O   . ASN   B 1 238 ? 10.754  31.257 39.248 1.000 28.259  ? 237 ASN   BBB O   1 ? 
ATOM   3915 C  CB  . ASN   B 1 238 ? 8.576   29.819 37.408 1.000 28.601  ? 237 ASN   BBB CB  1 ? 
ATOM   3916 C  CG  . ASN   B 1 238 ? 7.411   29.615 38.359 1.000 30.424  ? 237 ASN   BBB CG  1 ? 
ATOM   3917 O  OD1 . ASN   B 1 238 ? 6.343   30.211 38.200 1.000 36.062  ? 237 ASN   BBB OD1 1 ? 
ATOM   3918 N  ND2 . ASN   B 1 238 ? 7.618   28.791 39.379 1.000 41.385  ? 237 ASN   BBB ND2 1 ? 
ATOM   3919 N  N   . ALA   B 1 239 ? 8.725   32.215 39.667 1.000 31.878  ? 238 ALA   BBB N   1 ? 
ATOM   3920 C  CA  . ALA   B 1 239 ? 9.031   32.739 41.009 1.000 33.377  ? 238 ALA   BBB CA  1 ? 
ATOM   3921 C  C   . ALA   B 1 239 ? 9.238   31.570 41.978 1.000 28.508  ? 238 ALA   BBB C   1 ? 
ATOM   3922 O  O   . ALA   B 1 239 ? 8.359   30.704 42.111 1.000 40.734  ? 238 ALA   BBB O   1 ? 
ATOM   3923 C  CB  . ALA   B 1 239 ? 7.952   33.710 41.467 1.000 32.513  ? 238 ALA   BBB CB  1 ? 
ATOM   3924 N  N   . VAL   B 1 240 ? 10.411  31.537 42.608 1.000 29.314  ? 239 VAL   BBB N   1 ? 
ATOM   3925 C  CA  . VAL   B 1 240 ? 10.763  30.517 43.631 1.000 24.870  ? 239 VAL   BBB CA  1 ? 
ATOM   3926 C  C   . VAL   B 1 240 ? 11.056  31.210 44.953 1.000 23.163  ? 239 VAL   BBB C   1 ? 
ATOM   3927 O  O   . VAL   B 1 240 ? 12.120  31.827 45.133 1.000 25.467  ? 239 VAL   BBB O   1 ? 
ATOM   3928 C  CB  . VAL   B 1 240 ? 11.938  29.628 43.184 1.000 31.811  ? 239 VAL   BBB CB  1 ? 
ATOM   3929 C  CG1 . VAL   B 1 240 ? 12.252  28.603 44.266 1.000 39.070  ? 239 VAL   BBB CG1 1 ? 
ATOM   3930 C  CG2 . VAL   B 1 240 ? 11.678  28.969 41.831 1.000 31.360  ? 239 VAL   BBB CG2 1 ? 
ATOM   3931 N  N   . PRO   B 1 241 ? 10.093  31.190 45.893 1.000 23.755  ? 240 PRO   BBB N   1 ? 
ATOM   3932 C  CA  . PRO   B 1 241 ? 10.297  31.847 47.182 1.000 25.160  ? 240 PRO   BBB CA  1 ? 
ATOM   3933 C  C   . PRO   B 1 241 ? 11.497  31.279 47.938 1.000 22.416  ? 240 PRO   BBB C   1 ? 
ATOM   3934 O  O   . PRO   B 1 241 ? 11.768  30.109 47.870 1.000 26.856  ? 240 PRO   BBB O   1 ? 
ATOM   3935 C  CB  . PRO   B 1 241 ? 9.001   31.596 47.959 1.000 29.633  ? 240 PRO   BBB CB  1 ? 
ATOM   3936 C  CG  . PRO   B 1 241 ? 7.970   31.352 46.873 1.000 33.739  ? 240 PRO   BBB CG  1 ? 
ATOM   3937 C  CD  . PRO   B 1 241 ? 8.717   30.683 45.735 1.000 27.894  ? 240 PRO   BBB CD  1 ? 
ATOM   3938 N  N   . MET   B 1 242 ? 12.214  32.171 48.598 1.000 23.155  ? 241 MET   BBB N   1 ? 
ATOM   3939 C  CA  . MET   B 1 242 ? 13.331  31.867 49.538 1.000 22.416  ? 241 MET   BBB CA  1 ? 
ATOM   3940 C  C   . MET   B 1 242 ? 12.781  31.320 50.861 1.000 23.358  ? 241 MET   BBB C   1 ? 
ATOM   3941 O  O   . MET   B 1 242 ? 12.659  32.101 51.806 1.000 23.951  ? 241 MET   BBB O   1 ? 
ATOM   3942 C  CB  . MET   B 1 242 ? 14.132  33.116 49.869 1.000 26.586  ? 241 MET   BBB CB  1 ? 
ATOM   3943 C  CG  . MET   B 1 242 ? 15.366  33.301 49.127 1.000 32.168  ? 241 MET   BBB CG  1 ? 
ATOM   3944 S  SD  . MET   B 1 242 ? 16.086  34.885 49.659 1.000 27.100  ? 241 MET   BBB SD  1 ? 
ATOM   3945 C  CE  . MET   B 1 242 ? 16.460  35.483 48.013 1.000 24.635  ? 241 MET   BBB CE  1 ? 
ATOM   3946 N  N   . GLN   B 1 243 ? 12.431  30.026 50.958 1.000 24.201  ? 242 GLN   BBB N   1 ? 
ATOM   3947 C  CA  . GLN   B 1 243 ? 11.671  29.564 52.146 1.000 25.100  ? 242 GLN   BBB CA  1 ? 
ATOM   3948 C  C   . GLN   B 1 243 ? 12.576  29.418 53.370 1.000 24.439  ? 242 GLN   BBB C   1 ? 
ATOM   3949 O  O   . GLN   B 1 243 ? 12.053  29.515 54.490 1.000 24.510  ? 242 GLN   BBB O   1 ? 
ATOM   3950 C  CB  . GLN   B 1 243 ? 10.924  28.264 51.860 1.000 28.150  ? 242 GLN   BBB CB  1 ? 
ATOM   3951 C  CG  . GLN   B 1 243 ? 9.677   28.526 51.030 1.000 38.347  ? 242 GLN   BBB CG  1 ? 
ATOM   3952 C  CD  . GLN   B 1 243 ? 8.888   27.262 50.820 1.000 44.546  ? 242 GLN   BBB CD  1 ? 
ATOM   3953 O  OE1 . GLN   B 1 243 ? 8.488   26.952 49.707 1.000 55.372  ? 242 GLN   BBB OE1 1 ? 
ATOM   3954 N  NE2 . GLN   B 1 243 ? 8.709   26.506 51.892 1.000 44.414  ? 242 GLN   BBB NE2 1 ? 
ATOM   3955 N  N   . HIS   B 1 244 ? 13.876  29.185 53.205 1.000 21.865  ? 243 HIS   BBB N   1 ? 
ATOM   3956 C  CA  . HIS   B 1 244 ? 14.763  28.897 54.363 1.000 20.127  ? 243 HIS   BBB CA  1 ? 
ATOM   3957 C  C   . HIS   B 1 244 ? 16.221  28.986 53.953 1.000 17.530  ? 243 HIS   BBB C   1 ? 
ATOM   3958 O  O   . HIS   B 1 244 ? 16.525  28.807 52.756 1.000 21.226  ? 243 HIS   BBB O   1 ? 
ATOM   3959 C  CB  . HIS   B 1 244 ? 14.431  27.523 54.973 1.000 23.420  ? 243 HIS   BBB CB  1 ? 
ATOM   3960 C  CG  . HIS   B 1 244 ? 14.628  26.355 54.053 1.000 27.806  ? 243 HIS   BBB CG  1 ? 
ATOM   3961 N  ND1 . HIS   B 1 244 ? 15.812  25.677 53.988 1.000 33.639  ? 243 HIS   BBB ND1 1 ? 
ATOM   3962 C  CD2 . HIS   B 1 244 ? 13.796  25.754 53.163 1.000 33.099  ? 243 HIS   BBB CD2 1 ? 
ATOM   3963 C  CE1 . HIS   B 1 244 ? 15.701  24.679 53.123 1.000 40.825  ? 243 HIS   BBB CE1 1 ? 
ATOM   3964 N  NE2 . HIS   B 1 244 ? 14.472  24.706 52.590 1.000 41.151  ? 243 HIS   BBB NE2 1 ? 
ATOM   3965 N  N   . ASN   B 1 245 ? 17.087  29.249 54.926 1.000 18.733  ? 244 ASN   BBB N   1 ? 
ATOM   3966 C  CA  . ASN   B 1 245 ? 18.542  29.413 54.641 1.000 20.229  ? 244 ASN   BBB CA  1 ? 
ATOM   3967 C  C   . ASN   B 1 245 ? 19.342  29.259 55.942 1.000 21.144  ? 244 ASN   BBB C   1 ? 
ATOM   3968 O  O   . ASN   B 1 245 ? 20.434  29.839 56.022 1.000 22.398  ? 244 ASN   BBB O   1 ? 
ATOM   3969 C  CB  . ASN   B 1 245 ? 18.802  30.769 53.937 1.000 19.243  ? 244 ASN   BBB CB  1 ? 
ATOM   3970 C  CG  . ASN   B 1 245 ? 18.308  31.959 54.713 1.000 17.743  ? 244 ASN   BBB CG  1 ? 
ATOM   3971 O  OD1 . ASN   B 1 245 ? 18.018  31.825 55.911 1.000 18.965  ? 244 ASN   BBB OD1 1 ? 
ATOM   3972 N  ND2 . ASN   B 1 245 ? 18.349  33.136 54.037 1.000 19.499  ? 244 ASN   BBB ND2 1 ? 
ATOM   3973 N  N   . ASN   B 1 246 ? 18.896  28.381 56.861 1.000 18.666  ? 245 ASN   BBB N   1 ? 
ATOM   3974 C  CA  . ASN   B 1 246 ? 19.550  28.119 58.170 1.000 20.270  ? 245 ASN   BBB CA  1 ? 
ATOM   3975 C  C   . ASN   B 1 246 ? 20.261  26.768 58.113 1.000 20.791  ? 245 ASN   BBB C   1 ? 
ATOM   3976 O  O   . ASN   B 1 246 ? 19.609  25.757 57.723 1.000 25.583  ? 245 ASN   BBB O   1 ? 
ATOM   3977 C  CB  . ASN   B 1 246 ? 18.607  28.240 59.366 1.000 20.763  ? 245 ASN   BBB CB  1 ? 
ATOM   3978 C  CG  . ASN   B 1 246 ? 17.397  27.313 59.358 1.000 20.982  ? 245 ASN   BBB CG  1 ? 
ATOM   3979 O  OD1 . ASN   B 1 246 ? 17.125  26.677 60.367 1.000 37.695  ? 245 ASN   BBB OD1 1 ? 
ATOM   3980 N  ND2 . ASN   B 1 246 ? 16.714  27.149 58.232 1.000 22.389  ? 245 ASN   BBB ND2 1 ? 
ATOM   3981 N  N   . ARG   B 1 247 ? 21.554  26.794 58.414 1.000 22.545  ? 246 ARG   BBB N   1 ? 
ATOM   3982 C  CA  . ARG   B 1 247 ? 22.353  25.555 58.524 1.000 21.561  ? 246 ARG   BBB CA  1 ? 
ATOM   3983 C  C   . ARG   B 1 247 ? 22.057  24.912 59.871 1.000 21.573  ? 246 ARG   BBB C   1 ? 
ATOM   3984 O  O   . ARG   B 1 247 ? 21.974  25.529 60.917 1.000 22.072  ? 246 ARG   BBB O   1 ? 
ATOM   3985 C  CB  . ARG   B 1 247 ? 23.846  25.865 58.418 1.000 21.341  ? 246 ARG   BBB CB  1 ? 
ATOM   3986 C  CG  . ARG   B 1 247 ? 24.710  24.612 58.290 1.000 20.286  ? 246 ARG   BBB CG  1 ? 
ATOM   3987 C  CD  . ARG   B 1 247 ? 26.172  24.968 58.457 1.000 21.956  ? 246 ARG   BBB CD  1 ? 
ATOM   3988 N  NE  . ARG   B 1 247 ? 27.007  23.855 57.983 1.000 23.279  ? 246 ARG   BBB NE  1 ? 
ATOM   3989 C  CZ  . ARG   B 1 247 ? 28.322  23.759 58.133 1.000 20.520  ? 246 ARG   BBB CZ  1 ? 
ATOM   3990 N  NH1 . ARG   B 1 247 ? 29.022  24.635 58.805 1.000 21.499  ? 246 ARG   BBB NH1 1 ? 
ATOM   3991 N  NH2 . ARG   B 1 247 ? 28.988  22.702 57.664 1.000 26.669  ? 246 ARG   BBB NH2 1 ? 
ATOM   3992 N  N   . PRO   B 1 248 ? 21.934  23.550 59.927 1.000 22.842  ? 247 PRO   BBB N   1 ? 
ATOM   3993 C  CA  . PRO   B 1 248 ? 21.873  22.904 61.226 1.000 24.277  ? 247 PRO   BBB CA  1 ? 
ATOM   3994 C  C   . PRO   B 1 248 ? 23.132  23.143 62.092 1.000 25.051  ? 247 PRO   BBB C   1 ? 
ATOM   3995 O  O   . PRO   B 1 248 ? 24.234  23.389 61.540 1.000 23.916  ? 247 PRO   BBB O   1 ? 
ATOM   3996 C  CB  . PRO   B 1 248 ? 21.839  21.404 60.877 1.000 26.686  ? 247 PRO   BBB CB  1 ? 
ATOM   3997 C  CG  . PRO   B 1 248 ? 21.464  21.334 59.407 1.000 26.487  ? 247 PRO   BBB CG  1 ? 
ATOM   3998 C  CD  . PRO   B 1 248 ? 21.919  22.644 58.778 1.000 25.282  ? 247 PRO   BBB CD  1 ? 
ATOM   3999 N  N   . THR   B 1 249 ? 22.975  23.014 63.407 1.000 24.721  ? 248 THR   BBB N   1 ? 
ATOM   4000 C  CA  . THR   B 1 249 ? 24.160  23.010 64.319 1.000 22.939  ? 248 THR   BBB CA  1 ? 
ATOM   4001 C  C   . THR   B 1 249 ? 25.154  21.889 64.036 1.000 23.451  ? 248 THR   BBB C   1 ? 
ATOM   4002 O  O   . THR   B 1 249 ? 24.698  20.792 63.646 1.000 28.510  ? 248 THR   BBB O   1 ? 
ATOM   4003 C  CB  . THR   B 1 249 ? 23.695  23.124 65.782 1.000 22.643  ? 248 THR   BBB CB  1 ? 
ATOM   4004 O  OG1 . THR   B 1 249 ? 22.879  21.970 66.047 1.000 22.792  ? 248 THR   BBB OG1 1 ? 
ATOM   4005 C  CG2 . THR   B 1 249 ? 22.892  24.405 66.018 1.000 23.473  ? 248 THR   BBB CG2 1 ? 
ATOM   4006 N  N   . GLN   B 1 250 ? 26.418  22.207 64.250 1.000 24.193  ? 249 GLN   BBB N   1 ? 
ATOM   4007 C  CA  . GLN   B 1 250 ? 27.590  21.375 63.909 1.000 22.265  ? 249 GLN   BBB CA  1 ? 
ATOM   4008 C  C   . GLN   B 1 250 ? 28.288  21.030 65.210 1.000 26.020  ? 249 GLN   BBB C   1 ? 
ATOM   4009 O  O   . GLN   B 1 250 ? 28.165  21.699 66.255 1.000 26.938  ? 249 GLN   BBB O   1 ? 
ATOM   4010 C  CB  . GLN   B 1 250 ? 28.529  22.114 62.947 1.000 23.845  ? 249 GLN   BBB CB  1 ? 
ATOM   4011 C  CG  . GLN   B 1 250 ? 27.815  22.563 61.690 1.000 26.413  ? 249 GLN   BBB CG  1 ? 
ATOM   4012 C  CD  . GLN   B 1 250 ? 27.295  21.414 60.874 1.000 25.185  ? 249 GLN   BBB CD  1 ? 
ATOM   4013 O  OE1 . GLN   B 1 250 ? 28.011  20.434 60.664 1.000 28.635  ? 249 GLN   BBB OE1 1 ? 
ATOM   4014 N  NE2 . GLN   B 1 250 ? 26.064  21.541 60.365 1.000 29.103  ? 249 GLN   BBB NE2 1 ? 
ATOM   4015 N  N   . PRO   B 1 251 ? 29.047  19.923 65.168 1.000 28.732  ? 250 PRO   BBB N   1 ? 
ATOM   4016 C  CA  . PRO   B 1 251 ? 29.713  19.452 66.357 1.000 29.482  ? 250 PRO   BBB CA  1 ? 
ATOM   4017 C  C   . PRO   B 1 251 ? 30.747  20.448 66.891 1.000 28.541  ? 250 PRO   BBB C   1 ? 
ATOM   4018 O  O   . PRO   B 1 251 ? 31.575  20.939 66.126 1.000 28.804  ? 250 PRO   BBB O   1 ? 
ATOM   4019 C  CB  . PRO   B 1 251 ? 30.475  18.188 65.939 1.000 36.312  ? 250 PRO   BBB CB  1 ? 
ATOM   4020 C  CG  . PRO   B 1 251 ? 29.935  17.833 64.567 1.000 35.900  ? 250 PRO   BBB CG  1 ? 
ATOM   4021 C  CD  . PRO   B 1 251 ? 29.198  19.028 64.009 1.000 31.422  ? 250 PRO   BBB CD  1 ? 
ATOM   4022 N  N   . LEU   B 1 252 ? 30.726  20.558 68.215 1.000 30.232  ? 251 LEU   BBB N   1 ? 
ATOM   4023 C  CA  . LEU   B 1 252 ? 31.654  21.413 69.031 1.000 35.802  ? 251 LEU   BBB CA  1 ? 
ATOM   4024 C  C   . LEU   B 1 252 ? 33.080  20.840 68.924 1.000 28.576  ? 251 LEU   BBB C   1 ? 
ATOM   4025 O  O   . LEU   B 1 252 ? 34.023  21.684 68.879 1.000 28.796  ? 251 LEU   BBB O   1 ? 
ATOM   4026 C  CB  . LEU   B 1 252 ? 31.122  21.461 70.466 1.000 32.747  ? 251 LEU   BBB CB  1 ? 
ATOM   4027 C  CG  . LEU   B 1 252 ? 31.344  22.764 71.237 1.000 37.112  ? 251 LEU   BBB CG  1 ? 
ATOM   4028 C  CD1 . LEU   B 1 252 ? 31.000  23.992 70.418 1.000 36.335  ? 251 LEU   BBB CD1 1 ? 
ATOM   4029 C  CD2 . LEU   B 1 252 ? 30.538  22.757 72.534 1.000 42.020  ? 251 LEU   BBB CD2 1 ? 
ATOM   4030 N  N   . LYS   B 1 253 ? 33.268  19.488 68.825 1.000 30.710  ? 252 LYS   BBB N   1 ? 
ATOM   4031 C  CA  . LYS   B 1 253 ? 34.646  18.966 68.592 1.000 32.030  ? 252 LYS   BBB CA  1 ? 
ATOM   4032 C  C   . LYS   B 1 253 ? 35.663  19.686 69.551 1.000 34.762  ? 252 LYS   BBB C   1 ? 
ATOM   4033 O  O   . LYS   B 1 253 ? 36.783  19.840 69.134 1.000 42.009  ? 252 LYS   BBB O   1 ? 
ATOM   4034 C  CB  . LYS   B 1 253 ? 35.140  19.234 67.159 1.000 36.927  ? 252 LYS   BBB CB  1 ? 
ATOM   4035 C  CG  . LYS   B 1 253 ? 34.348  18.546 66.052 1.000 39.245  ? 252 LYS   BBB CG  1 ? 
ATOM   4036 C  CD  . LYS   B 1 253 ? 34.790  17.130 65.858 1.000 45.603  ? 252 LYS   BBB CD  1 ? 
ATOM   4037 C  CE  . LYS   B 1 253 ? 33.823  16.353 64.993 1.000 50.715  ? 252 LYS   BBB CE  1 ? 
ATOM   4038 N  NZ  . LYS   B 1 253 ? 33.777  16.904 63.618 1.000 60.802  ? 252 LYS   BBB NZ  1 ? 
ATOM   4039 N  N   . GLY   B 1 254 ? 35.210  19.668 70.849 1.000 31.672  ? 253 GLY   BBB N   1 ? 
ATOM   4040 C  CA  . GLY   B 1 254 ? 36.115  20.032 71.993 1.000 37.935  ? 253 GLY   BBB CA  1 ? 
ATOM   4041 C  C   . GLY   B 1 254 ? 36.292  21.531 72.185 1.000 33.027  ? 253 GLY   BBB C   1 ? 
ATOM   4042 O  O   . GLY   B 1 254 ? 36.979  21.887 73.124 1.000 30.650  ? 253 GLY   BBB O   1 ? 
ATOM   4043 N  N   . ARG   B 1 255 ? 35.655  22.365 71.350 1.000 32.371  ? 254 ARG   BBB N   1 ? 
ATOM   4044 C  CA  . ARG   B 1 255 ? 35.673  23.842 71.525 1.000 27.275  ? 254 ARG   BBB CA  1 ? 
ATOM   4045 C  C   . ARG   B 1 255 ? 34.942  24.211 72.810 1.000 26.057  ? 254 ARG   BBB C   1 ? 
ATOM   4046 O  O   . ARG   B 1 255 ? 33.972  23.507 73.196 1.000 28.157  ? 254 ARG   BBB O   1 ? 
ATOM   4047 C  CB  . ARG   B 1 255 ? 35.002  24.536 70.332 1.000 25.808  ? 254 ARG   BBB CB  1 ? 
ATOM   4048 C  CG  . ARG   B 1 255 ? 35.867  24.543 69.087 1.000 25.864  ? 254 ARG   BBB CG  1 ? 
ATOM   4049 C  CD  . ARG   B 1 255 ? 35.140  25.034 67.867 1.000 24.839  ? 254 ARG   BBB CD  1 ? 
ATOM   4050 N  NE  . ARG   B 1 255 ? 34.046  24.194 67.438 1.000 27.491  ? 254 ARG   BBB NE  1 ? 
ATOM   4051 C  CZ  . ARG   B 1 255 ? 33.152  24.518 66.541 1.000 24.332  ? 254 ARG   BBB CZ  1 ? 
ATOM   4052 N  NH1 . ARG   B 1 255 ? 33.138  25.736 66.033 1.000 21.615  ? 254 ARG   BBB NH1 1 ? 
ATOM   4053 N  NH2 . ARG   B 1 255 ? 32.212  23.680 66.176 1.000 24.579  ? 254 ARG   BBB NH2 1 ? 
ATOM   4054 N  N   . THR   B 1 256 ? 35.343  25.350 73.389 1.000 25.861  ? 255 THR   BBB N   1 ? 
ATOM   4055 C  CA  . THR   B 1 256 ? 34.708  25.937 74.584 1.000 27.412  ? 255 THR   BBB CA  1 ? 
ATOM   4056 C  C   . THR   B 1 256 ? 33.910  27.182 74.173 1.000 24.470  ? 255 THR   BBB C   1 ? 
ATOM   4057 O  O   . THR   B 1 256 ? 34.462  27.999 73.439 1.000 26.773  ? 255 THR   BBB O   1 ? 
ATOM   4058 C  CB  . THR   B 1 256 ? 35.745  26.335 75.636 1.000 32.885  ? 255 THR   BBB CB  1 ? 
ATOM   4059 O  OG1 . THR   B 1 256 ? 36.528  25.168 75.892 1.000 40.949  ? 255 THR   BBB OG1 1 ? 
ATOM   4060 C  CG2 . THR   B 1 256 ? 35.094  26.824 76.907 1.000 39.339  ? 255 THR   BBB CG2 1 ? 
ATOM   4061 N  N   . VAL   B 1 257 ? 32.657  27.259 74.607 1.000 23.703  ? 256 VAL   BBB N   1 ? 
ATOM   4062 C  CA  . VAL   B 1 257 ? 31.856  28.508 74.484 1.000 21.200  ? 256 VAL   BBB CA  1 ? 
ATOM   4063 C  C   . VAL   B 1 257 ? 32.076  29.311 75.763 1.000 21.637  ? 256 VAL   BBB C   1 ? 
ATOM   4064 O  O   . VAL   B 1 257 ? 31.736  28.842 76.849 1.000 22.403  ? 256 VAL   BBB O   1 ? 
ATOM   4065 C  CB  . VAL   B 1 257 ? 30.369  28.223 74.228 1.000 23.593  ? 256 VAL   BBB CB  1 ? 
ATOM   4066 C  CG1 . VAL   B 1 257 ? 29.603  29.523 74.125 1.000 24.038  ? 256 VAL   BBB CG1 1 ? 
ATOM   4067 C  CG2 . VAL   B 1 257 ? 30.136  27.360 72.993 1.000 22.721  ? 256 VAL   BBB CG2 1 ? 
ATOM   4068 N  N   . ARG   B 1 258 ? 32.709  30.484 75.647 1.000 20.405  ? 257 ARG   BBB N   1 ? 
ATOM   4069 C  CA  . ARG   B 1 258 ? 32.968  31.358 76.810 1.000 19.745  ? 257 ARG   BBB CA  1 ? 
ATOM   4070 C  C   . ARG   B 1 258 ? 31.782  32.334 76.964 1.000 20.478  ? 257 ARG   BBB C   1 ? 
ATOM   4071 O  O   . ARG   B 1 258 ? 31.111  32.646 75.950 1.000 23.692  ? 257 ARG   BBB O   1 ? 
ATOM   4072 C  CB  . ARG   B 1 258 ? 34.302  32.071 76.587 1.000 21.408  ? 257 ARG   BBB CB  1 ? 
ATOM   4073 C  CG  . ARG   B 1 258 ? 35.495  31.154 76.386 1.000 24.021  ? 257 ARG   BBB CG  1 ? 
ATOM   4074 C  CD  . ARG   B 1 258 ? 36.758  31.955 76.204 1.000 28.742  ? 257 ARG   BBB CD  1 ? 
ATOM   4075 N  NE  . ARG   B 1 258 ? 36.819  32.601 74.895 1.000 28.305  ? 257 ARG   BBB NE  1 ? 
ATOM   4076 C  CZ  . ARG   B 1 258 ? 37.539  33.680 74.616 1.000 28.232  ? 257 ARG   BBB CZ  1 ? 
ATOM   4077 N  NH1 . ARG   B 1 258 ? 38.294  34.278 75.530 1.000 33.726  ? 257 ARG   BBB NH1 1 ? 
ATOM   4078 N  NH2 . ARG   B 1 258 ? 37.537  34.135 73.389 1.000 28.583  ? 257 ARG   BBB NH2 1 ? 
ATOM   4079 N  N   . ALA   B 1 259 ? 31.491  32.704 78.206 1.000 19.799  ? 258 ALA   BBB N   1 ? 
ATOM   4080 C  CA  . ALA   B 1 259 ? 30.407  33.648 78.566 1.000 20.613  ? 258 ALA   BBB CA  1 ? 
ATOM   4081 C  C   . ALA   B 1 259 ? 31.042  34.925 79.111 1.000 20.167  ? 258 ALA   BBB C   1 ? 
ATOM   4082 O  O   . ALA   B 1 259 ? 32.005  34.835 79.878 1.000 22.065  ? 258 ALA   BBB O   1 ? 
ATOM   4083 C  CB  . ALA   B 1 259 ? 29.466  33.006 79.574 1.000 25.570  ? 258 ALA   BBB CB  1 ? 
ATOM   4084 N  N   . SER   B 1 260 ? 30.488  36.077 78.708 1.000 20.742  ? 259 SER   BBB N   1 ? 
ATOM   4085 C  CA  . SER   B 1 260 ? 30.902  37.405 79.236 1.000 21.594  ? 259 SER   BBB CA  1 ? 
ATOM   4086 C  C   . SER   B 1 260 ? 30.282  37.635 80.620 1.000 21.895  ? 259 SER   BBB C   1 ? 
ATOM   4087 O  O   . SER   B 1 260 ? 30.734  38.536 81.334 1.000 24.326  ? 259 SER   BBB O   1 ? 
ATOM   4088 C  CB  . SER   B 1 260 ? 30.546  38.504 78.281 1.000 22.602  ? 259 SER   BBB CB  1 ? 
ATOM   4089 O  OG  . SER   B 1 260 ? 29.160  38.783 78.356 1.000 22.562  ? 259 SER   BBB OG  1 ? 
ATOM   4090 N  N   . PHE   B 1 261 ? 29.319  36.801 81.017 1.000 22.304  ? 260 PHE   BBB N   1 ? 
ATOM   4091 C  CA  . PHE   B 1 261 ? 28.366  37.127 82.109 1.000 30.539  ? 260 PHE   BBB CA  1 ? 
ATOM   4092 C  C   . PHE   B 1 261 ? 28.165  35.904 83.000 1.000 35.790  ? 260 PHE   BBB C   1 ? 
ATOM   4093 O  O   . PHE   B 1 261 ? 27.598  36.045 84.066 1.000 38.734  ? 260 PHE   BBB O   1 ? 
ATOM   4094 C  CB  . PHE   B 1 261 ? 27.019  37.544 81.517 1.000 31.946  ? 260 PHE   BBB CB  1 ? 
ATOM   4095 C  CG  . PHE   B 1 261 ? 26.332  36.420 80.790 1.000 24.278  ? 260 PHE   BBB CG  1 ? 
ATOM   4096 C  CD1 . PHE   B 1 261 ? 26.638  36.173 79.462 1.000 22.201  ? 260 PHE   BBB CD1 1 ? 
ATOM   4097 C  CD2 . PHE   B 1 261 ? 25.434  35.592 81.439 1.000 28.414  ? 260 PHE   BBB CD2 1 ? 
ATOM   4098 C  CE1 . PHE   B 1 261 ? 25.974  35.197 78.751 1.000 26.785  ? 260 PHE   BBB CE1 1 ? 
ATOM   4099 C  CE2 . PHE   B 1 261 ? 24.820  34.553 80.749 1.000 28.549  ? 260 PHE   BBB CE2 1 ? 
ATOM   4100 C  CZ  . PHE   B 1 261 ? 25.089  34.361 79.410 1.000 27.149  ? 260 PHE   BBB CZ  1 ? 
ATOM   4101 O  OXT . PHE   B 1 261 ? 28.572  34.805 82.591 1.000 35.341  ? 260 PHE   BBB OXT 1 ? 
HETATM 4102 C  C   . ACT   C 2 .   ? -30.339 30.119 47.074 1.000 49.514  ? 301 ACT   AAA C   1 ? 
HETATM 4103 O  O   . ACT   C 2 .   ? -29.636 29.102 46.772 1.000 40.004  ? 301 ACT   AAA O   1 ? 
HETATM 4104 O  OXT . ACT   C 2 .   ? -29.872 31.267 47.236 1.000 41.711  ? 301 ACT   AAA OXT 1 ? 
HETATM 4105 C  CH3 . ACT   C 2 .   ? -31.853 29.989 47.240 1.000 40.014  ? 301 ACT   AAA CH3 1 ? 
HETATM 4106 C  C   . ACT   D 2 .   ? -34.975 33.304 36.456 1.000 61.409  ? 302 ACT   AAA C   1 ? 
HETATM 4107 O  O   . ACT   D 2 .   ? -34.474 34.201 35.732 1.000 62.783  ? 302 ACT   AAA O   1 ? 
HETATM 4108 O  OXT . ACT   D 2 .   ? -34.981 32.083 36.175 1.000 54.412  ? 302 ACT   AAA OXT 1 ? 
HETATM 4109 C  CH3 . ACT   D 2 .   ? -35.648 33.727 37.754 1.000 45.634  ? 302 ACT   AAA CH3 1 ? 
HETATM 4110 ZN ZN  . ZN    E 3 .   ? -13.533 34.921 39.751 1.000 19.492  ? 303 ZN    AAA ZN  1 ? 
HETATM 4111 C  C2  . A1H6C F 4 .   ? -20.723 37.256 44.235 1.000 42.889  ? 304 A1H6C AAA C2  1 ? 
HETATM 4112 C  C3  . A1H6C F 4 .   ? -21.369 37.693 45.531 1.000 35.399  ? 304 A1H6C AAA C3  1 ? 
HETATM 4113 C  C4  . A1H6C F 4 .   ? -22.867 37.376 45.569 1.000 41.077  ? 304 A1H6C AAA C4  1 ? 
HETATM 4114 C  C6  . A1H6C F 4 .   ? -22.822 35.117 47.145 1.000 44.077  ? 304 A1H6C AAA C6  1 ? 
HETATM 4115 C  C7  . A1H6C F 4 .   ? -23.916 34.904 47.975 1.000 54.719  ? 304 A1H6C AAA C7  1 ? 
HETATM 4116 C  C8  . A1H6C F 4 .   ? -23.723 34.488 49.281 1.000 56.587  ? 304 A1H6C AAA C8  1 ? 
HETATM 4117 C  C9  . A1H6C F 4 .   ? -22.442 34.277 49.792 1.000 55.302  ? 304 A1H6C AAA C9  1 ? 
HETATM 4118 C  C10 . A1H6C F 4 .   ? -22.243 33.797 51.209 1.000 56.318  ? 304 A1H6C AAA C10 1 ? 
HETATM 4119 C  C11 . A1H6C F 4 .   ? -21.352 34.499 48.945 1.000 53.073  ? 304 A1H6C AAA C11 1 ? 
HETATM 4120 C  C12 . A1H6C F 4 .   ? -21.532 34.914 47.636 1.000 46.068  ? 304 A1H6C AAA C12 1 ? 
HETATM 4121 C  C14 . A1H6C F 4 .   ? -18.772 36.381 43.222 1.000 33.497  ? 304 A1H6C AAA C14 1 ? 
HETATM 4122 C  C15 . A1H6C F 4 .   ? -18.124 35.164 43.357 1.000 33.295  ? 304 A1H6C AAA C15 1 ? 
HETATM 4123 C  C16 . A1H6C F 4 .   ? -17.415 34.631 42.289 1.000 26.351  ? 304 A1H6C AAA C16 1 ? 
HETATM 4124 C  C17 . A1H6C F 4 .   ? -17.363 35.325 41.093 1.000 24.808  ? 304 A1H6C AAA C17 1 ? 
HETATM 4125 O  O1  . A1H6C F 4 .   ? -21.295 37.237 43.161 1.000 45.246  ? 304 A1H6C AAA O1  1 ? 
HETATM 4126 S  S5  . A1H6C F 4 .   ? -23.144 35.583 45.490 1.000 41.591  ? 304 A1H6C AAA S5  1 ? 
HETATM 4127 O  O13 . A1H6C F 4 .   ? -19.421 36.880 44.377 1.000 46.333  ? 304 A1H6C AAA O13 1 ? 
HETATM 4128 S  S18 . A1H6C F 4 .   ? -16.530 34.633 39.702 1.000 19.227  ? 304 A1H6C AAA S18 1 ? 
HETATM 4129 O  O19 . A1H6C F 4 .   ? -16.181 35.763 38.837 1.000 22.514  ? 304 A1H6C AAA O19 1 ? 
HETATM 4130 N  N20 . A1H6C F 4 .   ? -15.180 34.022 40.170 1.000 18.275  ? 304 A1H6C AAA N20 1 ? 
HETATM 4131 O  O21 . A1H6C F 4 .   ? -17.421 33.602 39.180 1.000 20.775  ? 304 A1H6C AAA O21 1 ? 
HETATM 4132 C  C22 . A1H6C F 4 .   ? -18.013 36.547 40.944 1.000 26.379  ? 304 A1H6C AAA C22 1 ? 
HETATM 4133 C  C23 . A1H6C F 4 .   ? -18.720 37.077 42.013 1.000 27.587  ? 304 A1H6C AAA C23 1 ? 
HETATM 4134 ZN ZN  . ZN    G 3 .   ? 24.809  34.453 58.326 1.000 21.145  ? 301 ZN    BBB ZN  1 ? 
HETATM 4135 C  C2  . A1H6C H 4 .   ? 32.136  36.469 53.401 1.000 62.278  ? 302 A1H6C BBB C2  1 ? 
HETATM 4136 C  C3  . A1H6C H 4 .   ? 32.621  36.776 52.011 1.000 64.818  ? 302 A1H6C BBB C3  1 ? 
HETATM 4137 C  C4  . A1H6C H 4 .   ? 32.837  35.531 51.177 1.000 59.777  ? 302 A1H6C BBB C4  1 ? 
HETATM 4138 C  C6  . A1H6C H 4 .   ? 35.366  35.870 50.046 1.000 60.910  ? 302 A1H6C BBB C6  1 ? 
HETATM 4139 C  C7  . A1H6C H 4 .   ? 36.095  36.918 50.577 1.000 62.820  ? 302 A1H6C BBB C7  1 ? 
HETATM 4140 C  C8  . A1H6C H 4 .   ? 36.730  37.815 49.741 1.000 43.327  ? 302 A1H6C BBB C8  1 ? 
HETATM 4141 C  C9  . A1H6C H 4 .   ? 36.655  37.689 48.363 1.000 45.712  ? 302 A1H6C BBB C9  1 ? 
HETATM 4142 C  C10 . A1H6C H 4 .   ? 37.242  38.746 47.461 1.000 40.798  ? 302 A1H6C BBB C10 1 ? 
HETATM 4143 C  C11 . A1H6C H 4 .   ? 35.920  36.624 47.843 1.000 55.626  ? 302 A1H6C BBB C11 1 ? 
HETATM 4144 C  C12 . A1H6C H 4 .   ? 35.280  35.723 48.673 1.000 61.420  ? 302 A1H6C BBB C12 1 ? 
HETATM 4145 C  C14 . A1H6C H 4 .   ? 30.080  35.618 54.569 1.000 46.386  ? 302 A1H6C BBB C14 1 ? 
HETATM 4146 C  C15 . A1H6C H 4 .   ? 29.947  36.448 55.676 1.000 40.735  ? 302 A1H6C BBB C15 1 ? 
HETATM 4147 C  C16 . A1H6C H 4 .   ? 29.191  36.037 56.767 1.000 35.387  ? 302 A1H6C BBB C16 1 ? 
HETATM 4148 C  C17 . A1H6C H 4 .   ? 28.575  34.790 56.744 1.000 27.602  ? 302 A1H6C BBB C17 1 ? 
HETATM 4149 O  O1  . A1H6C H 4 .   ? 32.820  36.598 54.383 1.000 68.958  ? 302 A1H6C BBB O1  1 ? 
HETATM 4150 S  S5  . A1H6C H 4 .   ? 34.543  34.899 51.262 1.000 59.367  ? 302 A1H6C BBB S5  1 ? 
HETATM 4151 O  O13 . A1H6C H 4 .   ? 30.829  36.004 53.421 1.000 60.337  ? 302 A1H6C BBB O13 1 ? 
HETATM 4152 S  S18 . A1H6C H 4 .   ? 27.806  34.160 58.207 1.000 19.997  ? 302 A1H6C BBB S18 1 ? 
HETATM 4153 O  O19 . A1H6C H 4 .   ? 28.697  33.149 58.730 1.000 18.284  ? 302 A1H6C BBB O19 1 ? 
HETATM 4154 N  N20 . A1H6C H 4 .   ? 26.447  33.485 57.826 1.000 19.096  ? 302 A1H6C BBB N20 1 ? 
HETATM 4155 O  O21 . A1H6C H 4 .   ? 27.530  35.299 59.075 1.000 23.101  ? 302 A1H6C BBB O21 1 ? 
HETATM 4156 C  C22 . A1H6C H 4 .   ? 28.703  33.964 55.640 1.000 30.641  ? 302 A1H6C BBB C22 1 ? 
HETATM 4157 C  C23 . A1H6C H 4 .   ? 29.459  34.382 54.552 1.000 38.443  ? 302 A1H6C BBB C23 1 ? 
HETATM 4158 O  O   . HOH   I 5 .   ? -4.945  44.376 23.755 0.500 37.134  ? 401 HOH   AAA O   1 ? 
HETATM 4159 O  O   . HOH   I 5 .   ? -13.666 29.420 56.687 1.000 50.001  ? 402 HOH   AAA O   1 ? 
HETATM 4160 O  O   . HOH   I 5 .   ? -17.131 58.053 45.617 1.000 63.687  ? 403 HOH   AAA O   1 ? 
HETATM 4161 O  O   . HOH   I 5 .   ? -26.524 33.732 30.427 1.000 34.611  ? 404 HOH   AAA O   1 ? 
HETATM 4162 O  O   . HOH   I 5 .   ? -16.338 41.751 18.178 1.000 36.365  ? 405 HOH   AAA O   1 ? 
HETATM 4163 O  O   . HOH   I 5 .   ? -19.560 41.320 15.701 1.000 47.693  ? 406 HOH   AAA O   1 ? 
HETATM 4164 O  O   . HOH   I 5 .   ? -29.355 26.195 36.948 0.500 25.221  ? 407 HOH   AAA O   1 ? 
HETATM 4165 O  O   . HOH   I 5 .   ? -6.249  45.260 19.673 1.000 41.555  ? 408 HOH   AAA O   1 ? 
HETATM 4166 O  O   . HOH   I 5 .   ? 5.843   33.555 38.821 1.000 33.528  ? 409 HOH   AAA O   1 ? 
HETATM 4167 O  O   . HOH   I 5 .   ? -26.638 49.078 35.330 1.000 42.344  ? 410 HOH   AAA O   1 ? 
HETATM 4168 O  O   . HOH   I 5 .   ? 9.670   39.200 34.383 1.000 33.746  ? 411 HOH   AAA O   1 ? 
HETATM 4169 O  O   . HOH   I 5 .   ? -14.978 22.611 29.592 1.000 24.455  ? 412 HOH   AAA O   1 ? 
HETATM 4170 O  O   . HOH   I 5 .   ? -3.889  25.615 40.365 1.000 55.205  ? 413 HOH   AAA O   1 ? 
HETATM 4171 O  O   . HOH   I 5 .   ? -12.644 29.306 41.559 1.000 20.324  ? 414 HOH   AAA O   1 ? 
HETATM 4172 O  O   . HOH   I 5 .   ? 4.260   49.980 36.963 1.000 41.573  ? 415 HOH   AAA O   1 ? 
HETATM 4173 O  O   . HOH   I 5 .   ? -28.613 34.657 18.986 1.000 62.091  ? 416 HOH   AAA O   1 ? 
HETATM 4174 O  O   . HOH   I 5 .   ? -1.199  44.659 60.454 1.000 34.652  ? 417 HOH   AAA O   1 ? 
HETATM 4175 O  O   . HOH   I 5 .   ? -5.384  21.468 28.456 1.000 43.457  ? 418 HOH   AAA O   1 ? 
HETATM 4176 O  O   . HOH   I 5 .   ? -13.410 53.608 50.740 1.000 40.529  ? 419 HOH   AAA O   1 ? 
HETATM 4177 O  O   . HOH   I 5 .   ? -17.388 22.755 22.972 1.000 47.024  ? 420 HOH   AAA O   1 ? 
HETATM 4178 O  O   . HOH   I 5 .   ? 4.549   45.710 41.558 1.000 47.485  ? 421 HOH   AAA O   1 ? 
HETATM 4179 O  O   . HOH   I 5 .   ? -15.587 41.138 48.541 1.000 46.987  ? 422 HOH   AAA O   1 ? 
HETATM 4180 O  O   . HOH   I 5 .   ? -6.495  28.693 20.230 1.000 29.367  ? 423 HOH   AAA O   1 ? 
HETATM 4181 O  O   . HOH   I 5 .   ? 0.098   52.906 42.716 0.500 35.565  ? 424 HOH   AAA O   1 ? 
HETATM 4182 O  O   . HOH   I 5 .   ? 0.363   25.428 30.451 1.000 42.205  ? 425 HOH   AAA O   1 ? 
HETATM 4183 O  O   . HOH   I 5 .   ? 0.383   27.871 50.906 1.000 34.617  ? 426 HOH   AAA O   1 ? 
HETATM 4184 O  O   . HOH   I 5 .   ? -27.710 22.754 36.450 1.000 25.052  ? 427 HOH   AAA O   1 ? 
HETATM 4185 O  O   . HOH   I 5 .   ? -13.682 34.402 52.872 1.000 40.493  ? 428 HOH   AAA O   1 ? 
HETATM 4186 O  O   . HOH   I 5 .   ? -21.427 39.574 16.249 1.000 50.879  ? 429 HOH   AAA O   1 ? 
HETATM 4187 O  O   . HOH   I 5 .   ? -10.565 34.813 43.312 1.000 23.552  ? 430 HOH   AAA O   1 ? 
HETATM 4188 O  O   . HOH   I 5 .   ? -3.779  43.202 25.835 1.000 35.069  ? 431 HOH   AAA O   1 ? 
HETATM 4189 O  O   . HOH   I 5 .   ? -5.718  50.613 48.797 1.000 30.408  ? 432 HOH   AAA O   1 ? 
HETATM 4190 O  O   . HOH   I 5 .   ? -26.145 30.132 33.635 1.000 30.152  ? 433 HOH   AAA O   1 ? 
HETATM 4191 O  O   . HOH   I 5 .   ? -32.921 43.100 47.724 1.000 30.815  ? 434 HOH   AAA O   1 ? 
HETATM 4192 O  O   . HOH   I 5 .   ? -10.631 40.814 23.242 1.000 23.528  ? 435 HOH   AAA O   1 ? 
HETATM 4193 O  O   . HOH   I 5 .   ? -10.636 48.183 26.017 1.000 33.676  ? 436 HOH   AAA O   1 ? 
HETATM 4194 O  O   . HOH   I 5 .   ? -6.908  25.531 42.442 1.000 31.908  ? 437 HOH   AAA O   1 ? 
HETATM 4195 O  O   . HOH   I 5 .   ? -21.705 51.201 29.199 1.000 39.083  ? 438 HOH   AAA O   1 ? 
HETATM 4196 O  O   . HOH   I 5 .   ? -5.380  38.168 64.019 1.000 34.379  ? 439 HOH   AAA O   1 ? 
HETATM 4197 O  O   . HOH   I 5 .   ? -21.292 19.221 35.254 1.000 40.156  ? 440 HOH   AAA O   1 ? 
HETATM 4198 O  O   . HOH   I 5 .   ? 8.617   42.092 36.878 1.000 38.469  ? 441 HOH   AAA O   1 ? 
HETATM 4199 O  O   . HOH   I 5 .   ? -5.341  31.793 60.321 1.000 34.993  ? 442 HOH   AAA O   1 ? 
HETATM 4200 O  O   . HOH   I 5 .   ? -15.657 55.314 47.445 1.000 33.126  ? 443 HOH   AAA O   1 ? 
HETATM 4201 O  O   . HOH   I 5 .   ? 1.217   40.638 48.318 1.000 30.376  ? 444 HOH   AAA O   1 ? 
HETATM 4202 O  O   . HOH   I 5 .   ? -15.173 32.897 15.525 1.000 46.016  ? 445 HOH   AAA O   1 ? 
HETATM 4203 O  O   . HOH   I 5 .   ? -5.057  47.730 56.278 1.000 40.660  ? 446 HOH   AAA O   1 ? 
HETATM 4204 O  O   . HOH   I 5 .   ? 9.928   35.830 39.228 1.000 30.149  ? 447 HOH   AAA O   1 ? 
HETATM 4205 O  O   . HOH   I 5 .   ? 6.298   46.610 31.179 1.000 41.230  ? 448 HOH   AAA O   1 ? 
HETATM 4206 O  O   . HOH   I 5 .   ? -0.051  31.339 38.001 1.000 25.534  ? 449 HOH   AAA O   1 ? 
HETATM 4207 O  O   . HOH   I 5 .   ? -12.530 59.358 41.938 1.000 39.150  ? 450 HOH   AAA O   1 ? 
HETATM 4208 O  O   . HOH   I 5 .   ? 7.595   37.624 33.247 1.000 28.883  ? 451 HOH   AAA O   1 ? 
HETATM 4209 O  O   . HOH   I 5 .   ? -15.512 60.640 38.698 1.000 42.458  ? 452 HOH   AAA O   1 ? 
HETATM 4210 O  O   . HOH   I 5 .   ? -9.516  21.783 23.737 1.000 39.798  ? 453 HOH   AAA O   1 ? 
HETATM 4211 O  O   . HOH   I 5 .   ? -15.979 37.059 44.191 1.000 34.302  ? 454 HOH   AAA O   1 ? 
HETATM 4212 O  O   . HOH   I 5 .   ? -37.064 39.291 44.237 1.000 36.875  ? 455 HOH   AAA O   1 ? 
HETATM 4213 O  O   . HOH   I 5 .   ? -4.925  50.637 35.676 1.000 35.703  ? 456 HOH   AAA O   1 ? 
HETATM 4214 O  O   . HOH   I 5 .   ? -13.043 20.876 30.461 1.000 30.988  ? 457 HOH   AAA O   1 ? 
HETATM 4215 O  O   . HOH   I 5 .   ? -26.220 22.544 29.846 1.000 37.092  ? 458 HOH   AAA O   1 ? 
HETATM 4216 O  O   . HOH   I 5 .   ? 4.174   36.607 52.018 1.000 26.364  ? 459 HOH   AAA O   1 ? 
HETATM 4217 O  O   . HOH   I 5 .   ? -20.646 58.067 36.304 1.000 45.332  ? 460 HOH   AAA O   1 ? 
HETATM 4218 O  O   . HOH   I 5 .   ? -5.070  29.718 23.472 1.000 25.883  ? 461 HOH   AAA O   1 ? 
HETATM 4219 O  O   . HOH   I 5 .   ? -4.842  46.613 29.105 1.000 57.292  ? 462 HOH   AAA O   1 ? 
HETATM 4220 O  O   . HOH   I 5 .   ? -36.223 36.696 37.610 1.000 46.261  ? 463 HOH   AAA O   1 ? 
HETATM 4221 O  O   . HOH   I 5 .   ? -20.589 50.489 40.463 1.000 25.181  ? 464 HOH   AAA O   1 ? 
HETATM 4222 O  O   . HOH   I 5 .   ? -13.320 56.169 44.684 1.000 32.098  ? 465 HOH   AAA O   1 ? 
HETATM 4223 O  O   . HOH   I 5 .   ? 1.419   35.149 59.377 1.000 35.659  ? 466 HOH   AAA O   1 ? 
HETATM 4224 O  O   . HOH   I 5 .   ? -9.233  23.121 30.351 1.000 27.574  ? 467 HOH   AAA O   1 ? 
HETATM 4225 O  O   . HOH   I 5 .   ? -19.459 20.465 36.878 1.000 35.894  ? 468 HOH   AAA O   1 ? 
HETATM 4226 O  O   . HOH   I 5 .   ? -26.811 36.396 33.562 1.000 23.898  ? 469 HOH   AAA O   1 ? 
HETATM 4227 O  O   . HOH   I 5 .   ? 3.678   46.808 44.424 1.000 35.082  ? 470 HOH   AAA O   1 ? 
HETATM 4228 O  O   . HOH   I 5 .   ? -4.819  29.580 55.884 1.000 38.844  ? 471 HOH   AAA O   1 ? 
HETATM 4229 O  O   . HOH   I 5 .   ? -22.210 52.379 39.704 1.000 26.019  ? 472 HOH   AAA O   1 ? 
HETATM 4230 O  O   . HOH   I 5 .   ? -0.843  39.394 26.571 1.000 27.773  ? 473 HOH   AAA O   1 ? 
HETATM 4231 O  O   . HOH   I 5 .   ? -22.807 53.341 42.536 1.000 26.481  ? 474 HOH   AAA O   1 ? 
HETATM 4232 O  O   . HOH   I 5 .   ? 3.772   33.377 27.943 1.000 28.988  ? 475 HOH   AAA O   1 ? 
HETATM 4233 O  O   . HOH   I 5 .   ? -13.277 35.637 44.275 1.000 24.558  ? 476 HOH   AAA O   1 ? 
HETATM 4234 O  O   . HOH   I 5 .   ? -9.046  25.839 34.889 1.000 22.786  ? 477 HOH   AAA O   1 ? 
HETATM 4235 O  O   . HOH   I 5 .   ? -26.685 43.967 23.108 1.000 36.362  ? 478 HOH   AAA O   1 ? 
HETATM 4236 O  O   . HOH   I 5 .   ? -6.035  56.074 41.987 1.000 42.725  ? 479 HOH   AAA O   1 ? 
HETATM 4237 O  O   . HOH   I 5 .   ? -7.922  38.448 43.482 1.000 19.989  ? 480 HOH   AAA O   1 ? 
HETATM 4238 O  O   . HOH   I 5 .   ? 1.821   38.399 27.846 1.000 26.492  ? 481 HOH   AAA O   1 ? 
HETATM 4239 O  O   . HOH   I 5 .   ? 0.505   32.500 30.565 1.000 22.459  ? 482 HOH   AAA O   1 ? 
HETATM 4240 O  O   . HOH   I 5 .   ? -8.697  37.282 27.553 1.000 20.496  ? 483 HOH   AAA O   1 ? 
HETATM 4241 O  O   . HOH   I 5 .   ? -18.889 43.847 46.207 0.500 32.193  ? 484 HOH   AAA O   1 ? 
HETATM 4242 O  O   . HOH   I 5 .   ? 4.067   40.325 27.370 1.000 32.668  ? 485 HOH   AAA O   1 ? 
HETATM 4243 O  O   . HOH   I 5 .   ? -24.142 33.729 26.207 1.000 30.916  ? 486 HOH   AAA O   1 ? 
HETATM 4244 O  O   . HOH   I 5 .   ? -20.346 17.914 28.471 1.000 48.630  ? 487 HOH   AAA O   1 ? 
HETATM 4245 O  O   . HOH   I 5 .   ? -1.041  41.184 59.024 1.000 24.957  ? 488 HOH   AAA O   1 ? 
HETATM 4246 O  O   . HOH   I 5 .   ? -14.124 31.515 18.015 1.000 36.395  ? 489 HOH   AAA O   1 ? 
HETATM 4247 O  O   . HOH   I 5 .   ? -33.080 47.140 30.578 1.000 63.702  ? 490 HOH   AAA O   1 ? 
HETATM 4248 O  O   . HOH   I 5 .   ? -19.591 46.189 46.247 0.500 27.418  ? 491 HOH   AAA O   1 ? 
HETATM 4249 O  O   . HOH   I 5 .   ? -4.223  45.284 31.333 1.000 26.625  ? 492 HOH   AAA O   1 ? 
HETATM 4250 O  O   . HOH   I 5 .   ? -23.837 16.419 45.803 1.000 44.869  ? 493 HOH   AAA O   1 ? 
HETATM 4251 O  O   . HOH   I 5 .   ? -25.792 26.958 45.276 1.000 29.829  ? 494 HOH   AAA O   1 ? 
HETATM 4252 O  O   . HOH   I 5 .   ? 4.944   40.585 47.940 1.000 43.675  ? 495 HOH   AAA O   1 ? 
HETATM 4253 O  O   . HOH   I 5 .   ? -18.830 20.843 50.511 1.000 49.178  ? 496 HOH   AAA O   1 ? 
HETATM 4254 O  O   . HOH   I 5 .   ? -5.538  39.213 59.559 1.000 23.883  ? 497 HOH   AAA O   1 ? 
HETATM 4255 O  O   . HOH   I 5 .   ? 2.088   45.752 47.904 1.000 34.268  ? 498 HOH   AAA O   1 ? 
HETATM 4256 O  O   . HOH   I 5 .   ? -1.852  29.287 59.931 1.000 35.118  ? 499 HOH   AAA O   1 ? 
HETATM 4257 O  O   . HOH   I 5 .   ? -17.091 18.979 43.803 1.000 38.260  ? 500 HOH   AAA O   1 ? 
HETATM 4258 O  O   . HOH   I 5 .   ? -3.392  34.929 65.389 1.000 33.767  ? 501 HOH   AAA O   1 ? 
HETATM 4259 O  O   . HOH   I 5 .   ? -10.998 19.911 33.922 1.000 28.517  ? 502 HOH   AAA O   1 ? 
HETATM 4260 O  O   . HOH   I 5 .   ? 6.248   42.718 40.680 1.000 28.010  ? 503 HOH   AAA O   1 ? 
HETATM 4261 O  O   . HOH   I 5 .   ? 0.278   29.624 31.405 1.000 31.220  ? 504 HOH   AAA O   1 ? 
HETATM 4262 O  O   . HOH   I 5 .   ? -6.272  30.639 47.715 1.000 43.565  ? 505 HOH   AAA O   1 ? 
HETATM 4263 O  O   . HOH   I 5 .   ? -3.262  41.199 23.643 1.000 53.580  ? 506 HOH   AAA O   1 ? 
HETATM 4264 O  O   . HOH   I 5 .   ? -21.724 22.237 33.762 1.000 29.811  ? 507 HOH   AAA O   1 ? 
HETATM 4265 O  O   . HOH   I 5 .   ? -16.538 46.932 50.188 1.000 33.313  ? 508 HOH   AAA O   1 ? 
HETATM 4266 O  O   . HOH   I 5 .   ? -10.852 32.512 44.470 1.000 21.416  ? 509 HOH   AAA O   1 ? 
HETATM 4267 O  O   . HOH   I 5 .   ? 8.625   43.286 32.054 1.000 35.410  ? 510 HOH   AAA O   1 ? 
HETATM 4268 O  O   . HOH   I 5 .   ? -19.680 60.230 42.048 1.000 38.168  ? 511 HOH   AAA O   1 ? 
HETATM 4269 O  O   . HOH   I 5 .   ? -15.971 24.722 23.989 1.000 38.020  ? 512 HOH   AAA O   1 ? 
HETATM 4270 O  O   . HOH   I 5 .   ? -29.685 28.840 35.933 1.000 41.604  ? 513 HOH   AAA O   1 ? 
HETATM 4271 O  O   . HOH   I 5 .   ? -0.982  44.173 55.653 1.000 22.474  ? 514 HOH   AAA O   1 ? 
HETATM 4272 O  O   . HOH   I 5 .   ? 2.859   34.826 66.089 1.000 38.221  ? 515 HOH   AAA O   1 ? 
HETATM 4273 O  O   . HOH   I 5 .   ? 7.406   39.914 43.316 1.000 29.508  ? 516 HOH   AAA O   1 ? 
HETATM 4274 O  O   . HOH   I 5 .   ? -14.773 53.638 31.849 1.000 30.405  ? 517 HOH   AAA O   1 ? 
HETATM 4275 O  O   . HOH   I 5 .   ? -25.747 27.502 25.569 1.000 38.632  ? 518 HOH   AAA O   1 ? 
HETATM 4276 O  O   . HOH   I 5 .   ? -16.790 26.120 22.078 1.000 34.473  ? 519 HOH   AAA O   1 ? 
HETATM 4277 O  O   . HOH   I 5 .   ? -11.789 50.493 54.126 1.000 30.442  ? 520 HOH   AAA O   1 ? 
HETATM 4278 O  O   . HOH   I 5 .   ? 3.983   45.855 39.284 1.000 39.801  ? 521 HOH   AAA O   1 ? 
HETATM 4279 O  O   . HOH   I 5 .   ? -27.126 46.195 27.198 1.000 38.859  ? 522 HOH   AAA O   1 ? 
HETATM 4280 O  O   . HOH   I 5 .   ? -2.561  48.142 57.932 1.000 30.542  ? 523 HOH   AAA O   1 ? 
HETATM 4281 O  O   . HOH   I 5 .   ? -7.574  50.062 56.669 1.000 45.365  ? 524 HOH   AAA O   1 ? 
HETATM 4282 O  O   . HOH   I 5 .   ? -17.147 44.066 21.889 1.000 28.077  ? 525 HOH   AAA O   1 ? 
HETATM 4283 O  O   . HOH   I 5 .   ? -16.496 46.640 22.054 1.000 47.602  ? 526 HOH   AAA O   1 ? 
HETATM 4284 O  O   . HOH   I 5 .   ? -24.036 31.489 24.362 1.000 36.920  ? 527 HOH   AAA O   1 ? 
HETATM 4285 O  O   . HOH   I 5 .   ? -26.535 45.644 45.807 1.000 28.921  ? 528 HOH   AAA O   1 ? 
HETATM 4286 O  O   . HOH   I 5 .   ? -15.267 21.773 41.142 1.000 35.770  ? 529 HOH   AAA O   1 ? 
HETATM 4287 O  O   . HOH   I 5 .   ? -13.399 56.975 33.668 1.000 60.596  ? 530 HOH   AAA O   1 ? 
HETATM 4288 O  O   . HOH   I 5 .   ? -0.836  46.874 29.939 1.000 40.001  ? 531 HOH   AAA O   1 ? 
HETATM 4289 O  O   . HOH   I 5 .   ? -30.053 41.336 29.077 1.000 53.057  ? 532 HOH   AAA O   1 ? 
HETATM 4290 O  O   . HOH   I 5 .   ? -4.079  49.184 50.500 1.000 37.856  ? 533 HOH   AAA O   1 ? 
HETATM 4291 O  O   . HOH   I 5 .   ? -24.360 16.041 49.837 1.000 42.511  ? 534 HOH   AAA O   1 ? 
HETATM 4292 O  O   . HOH   I 5 .   ? -8.777  58.546 48.805 1.000 31.945  ? 535 HOH   AAA O   1 ? 
HETATM 4293 O  O   . HOH   I 5 .   ? -2.465  51.535 45.781 1.000 33.274  ? 536 HOH   AAA O   1 ? 
HETATM 4294 O  O   . HOH   I 5 .   ? -7.884  49.395 28.265 1.000 50.316  ? 537 HOH   AAA O   1 ? 
HETATM 4295 O  O   . HOH   I 5 .   ? -27.364 32.158 32.604 1.000 33.769  ? 538 HOH   AAA O   1 ? 
HETATM 4296 O  O   . HOH   I 5 .   ? -19.418 25.824 21.640 1.000 34.887  ? 539 HOH   AAA O   1 ? 
HETATM 4297 O  O   . HOH   I 5 .   ? 5.494   34.495 45.865 1.000 27.620  ? 540 HOH   AAA O   1 ? 
HETATM 4298 O  O   . HOH   I 5 .   ? -4.302  24.739 21.296 1.000 28.026  ? 541 HOH   AAA O   1 ? 
HETATM 4299 O  O   . HOH   I 5 .   ? 3.198   44.155 54.262 1.000 32.690  ? 542 HOH   AAA O   1 ? 
HETATM 4300 O  O   . HOH   I 5 .   ? -1.509  24.975 28.653 1.000 32.328  ? 543 HOH   AAA O   1 ? 
HETATM 4301 O  O   . HOH   I 5 .   ? 6.955   43.182 37.918 1.000 37.009  ? 544 HOH   AAA O   1 ? 
HETATM 4302 O  O   . HOH   I 5 .   ? -16.271 49.997 26.159 1.000 39.745  ? 545 HOH   AAA O   1 ? 
HETATM 4303 O  O   . HOH   I 5 .   ? -1.199  43.890 28.511 1.000 28.044  ? 546 HOH   AAA O   1 ? 
HETATM 4304 O  O   . HOH   I 5 .   ? -8.112  54.521 36.799 1.000 31.104  ? 547 HOH   AAA O   1 ? 
HETATM 4305 O  O   . HOH   I 5 .   ? -13.266 46.168 20.431 1.000 46.321  ? 548 HOH   AAA O   1 ? 
HETATM 4306 O  O   . HOH   I 5 .   ? -26.781 28.624 47.474 1.000 35.972  ? 549 HOH   AAA O   1 ? 
HETATM 4307 O  O   . HOH   I 5 .   ? -27.157 43.247 47.988 1.000 28.224  ? 550 HOH   AAA O   1 ? 
HETATM 4308 O  O   . HOH   I 5 .   ? -21.375 30.011 49.925 1.000 34.378  ? 551 HOH   AAA O   1 ? 
HETATM 4309 O  O   . HOH   I 5 .   ? -31.095 48.793 31.236 1.000 41.240  ? 552 HOH   AAA O   1 ? 
HETATM 4310 O  O   . HOH   I 5 .   ? 5.548   32.591 43.676 1.000 26.205  ? 553 HOH   AAA O   1 ? 
HETATM 4311 O  O   . HOH   I 5 .   ? -15.498 22.322 50.670 1.000 40.117  ? 554 HOH   AAA O   1 ? 
HETATM 4312 O  O   . HOH   I 5 .   ? -10.368 52.865 29.964 1.000 40.702  ? 555 HOH   AAA O   1 ? 
HETATM 4313 O  O   . HOH   I 5 .   ? -11.718 49.208 28.144 1.000 45.136  ? 556 HOH   AAA O   1 ? 
HETATM 4314 O  O   . HOH   I 5 .   ? -28.005 28.020 40.641 1.000 28.705  ? 557 HOH   AAA O   1 ? 
HETATM 4315 O  O   . HOH   I 5 .   ? -6.770  54.343 47.214 1.000 32.288  ? 558 HOH   AAA O   1 ? 
HETATM 4316 O  O   . HOH   I 5 .   ? 6.834   31.006 32.716 1.000 35.554  ? 559 HOH   AAA O   1 ? 
HETATM 4317 O  O   . HOH   I 5 .   ? -0.961  29.051 63.270 1.000 43.000  ? 560 HOH   AAA O   1 ? 
HETATM 4318 O  O   . HOH   I 5 .   ? 2.876   42.562 47.417 1.000 36.027  ? 561 HOH   AAA O   1 ? 
HETATM 4319 O  O   . HOH   I 5 .   ? -2.884  27.808 48.603 1.000 46.343  ? 562 HOH   AAA O   1 ? 
HETATM 4320 O  O   . HOH   I 5 .   ? -3.056  22.386 35.475 1.000 55.116  ? 563 HOH   AAA O   1 ? 
HETATM 4321 O  O   . HOH   I 5 .   ? -17.137 42.244 15.454 1.000 41.749  ? 564 HOH   AAA O   1 ? 
HETATM 4322 O  O   . HOH   I 5 .   ? -9.461  22.328 21.052 1.000 43.915  ? 565 HOH   AAA O   1 ? 
HETATM 4323 O  O   . HOH   I 5 .   ? -19.541 31.268 50.158 0.500 33.360  ? 566 HOH   AAA O   1 ? 
HETATM 4324 O  O   . HOH   I 5 .   ? -14.868 19.013 31.818 1.000 39.235  ? 567 HOH   AAA O   1 ? 
HETATM 4325 O  O   . HOH   I 5 .   ? -8.859  21.989 34.234 1.000 37.422  ? 568 HOH   AAA O   1 ? 
HETATM 4326 O  O   . HOH   I 5 .   ? 4.739   47.622 35.346 1.000 40.666  ? 569 HOH   AAA O   1 ? 
HETATM 4327 O  O   . HOH   I 5 .   ? 1.547   42.921 63.728 1.000 41.104  ? 570 HOH   AAA O   1 ? 
HETATM 4328 O  O   . HOH   I 5 .   ? -25.697 24.121 45.575 1.000 31.167  ? 571 HOH   AAA O   1 ? 
HETATM 4329 O  O   . HOH   I 5 .   ? 4.766   33.370 48.161 1.000 33.705  ? 572 HOH   AAA O   1 ? 
HETATM 4330 O  O   . HOH   I 5 .   ? 4.834   39.140 52.783 1.000 30.593  ? 573 HOH   AAA O   1 ? 
HETATM 4331 O  O   . HOH   I 5 .   ? -13.751 20.428 53.919 1.000 48.791  ? 574 HOH   AAA O   1 ? 
HETATM 4332 O  O   . HOH   I 5 .   ? -15.778 32.100 51.945 1.000 46.294  ? 575 HOH   AAA O   1 ? 
HETATM 4333 O  O   . HOH   I 5 .   ? -28.204 21.235 42.733 1.000 35.389  ? 576 HOH   AAA O   1 ? 
HETATM 4334 O  O   . HOH   I 5 .   ? -15.444 35.262 48.976 1.000 41.799  ? 577 HOH   AAA O   1 ? 
HETATM 4335 O  O   . HOH   I 5 .   ? -27.533 36.052 26.800 1.000 49.486  ? 578 HOH   AAA O   1 ? 
HETATM 4336 O  O   . HOH   I 5 .   ? -8.874  42.709 60.355 1.000 48.165  ? 579 HOH   AAA O   1 ? 
HETATM 4337 O  O   . HOH   I 5 .   ? 3.212   42.826 26.760 1.000 55.477  ? 580 HOH   AAA O   1 ? 
HETATM 4338 O  O   . HOH   I 5 .   ? -27.085 30.550 22.041 1.000 78.792  ? 581 HOH   AAA O   1 ? 
HETATM 4339 O  O   . HOH   I 5 .   ? -35.965 46.925 39.958 1.000 50.684  ? 582 HOH   AAA O   1 ? 
HETATM 4340 O  O   . HOH   I 5 .   ? -7.362  22.723 32.220 1.000 34.192  ? 583 HOH   AAA O   1 ? 
HETATM 4341 O  O   . HOH   I 5 .   ? -26.258 30.321 24.604 1.000 37.977  ? 584 HOH   AAA O   1 ? 
HETATM 4342 O  O   . HOH   I 5 .   ? 6.138   46.101 37.390 1.000 40.868  ? 585 HOH   AAA O   1 ? 
HETATM 4343 O  O   . HOH   I 5 .   ? -17.999 43.075 19.383 1.000 41.759  ? 586 HOH   AAA O   1 ? 
HETATM 4344 O  O   . HOH   I 5 .   ? -26.364 33.345 27.735 1.000 35.639  ? 587 HOH   AAA O   1 ? 
HETATM 4345 O  O   . HOH   I 5 .   ? 5.301   29.077 32.146 1.000 48.977  ? 588 HOH   AAA O   1 ? 
HETATM 4346 O  O   . HOH   I 5 .   ? -3.264  46.165 61.610 1.000 37.574  ? 589 HOH   AAA O   1 ? 
HETATM 4347 O  O   . HOH   I 5 .   ? -13.220 52.025 53.069 1.000 42.952  ? 590 HOH   AAA O   1 ? 
HETATM 4348 O  O   . HOH   I 5 .   ? -35.676 40.385 46.624 1.000 28.256  ? 591 HOH   AAA O   1 ? 
HETATM 4349 O  O   . HOH   I 5 .   ? -29.703 26.117 39.545 1.000 45.561  ? 592 HOH   AAA O   1 ? 
HETATM 4350 O  O   . HOH   I 5 .   ? -29.664 35.763 30.321 1.000 46.175  ? 593 HOH   AAA O   1 ? 
HETATM 4351 O  O   . HOH   I 5 .   ? 4.221   43.424 51.723 1.000 44.770  ? 594 HOH   AAA O   1 ? 
HETATM 4352 O  O   . HOH   I 5 .   ? 0.641   42.718 57.443 1.000 24.891  ? 595 HOH   AAA O   1 ? 
HETATM 4353 O  O   . HOH   I 5 .   ? -7.982  31.549 60.652 1.000 43.033  ? 596 HOH   AAA O   1 ? 
HETATM 4354 O  O   . HOH   I 5 .   ? -32.543 45.668 48.924 1.000 55.577  ? 597 HOH   AAA O   1 ? 
HETATM 4355 O  O   . HOH   I 5 .   ? -7.162  21.606 20.013 1.000 44.129  ? 598 HOH   AAA O   1 ? 
HETATM 4356 O  O   . HOH   I 5 .   ? -10.373 18.489 31.335 1.000 54.930  ? 599 HOH   AAA O   1 ? 
HETATM 4357 O  O   . HOH   I 5 .   ? 8.360   42.329 42.286 1.000 31.257  ? 600 HOH   AAA O   1 ? 
HETATM 4358 O  O   . HOH   I 5 .   ? -13.469 50.937 27.420 1.000 45.483  ? 601 HOH   AAA O   1 ? 
HETATM 4359 O  O   . HOH   I 5 .   ? 1.552   44.740 59.014 1.000 37.113  ? 602 HOH   AAA O   1 ? 
HETATM 4360 O  O   . HOH   I 5 .   ? -2.179  28.731 21.944 1.000 38.870  ? 603 HOH   AAA O   1 ? 
HETATM 4361 O  O   . HOH   I 5 .   ? -30.453 28.640 33.195 1.000 41.992  ? 604 HOH   AAA O   1 ? 
HETATM 4362 O  O   . HOH   I 5 .   ? -4.376  29.773 58.868 1.000 39.995  ? 605 HOH   AAA O   1 ? 
HETATM 4363 O  O   . HOH   I 5 .   ? -4.188  27.319 20.737 1.000 29.534  ? 606 HOH   AAA O   1 ? 
HETATM 4364 O  O   . HOH   I 5 .   ? -28.611 44.182 50.031 1.000 56.087  ? 607 HOH   AAA O   1 ? 
HETATM 4365 O  O   . HOH   I 5 .   ? -6.503  41.193 61.152 1.000 36.622  ? 608 HOH   AAA O   1 ? 
HETATM 4366 O  O   . HOH   I 5 .   ? -27.733 27.117 43.260 1.000 35.227  ? 609 HOH   AAA O   1 ? 
HETATM 4367 O  O   . HOH   I 5 .   ? -12.229 31.846 16.589 1.000 50.729  ? 610 HOH   AAA O   1 ? 
HETATM 4368 O  O   . HOH   I 5 .   ? -28.458 21.151 38.534 1.000 38.303  ? 611 HOH   AAA O   1 ? 
HETATM 4369 O  O   . HOH   I 5 .   ? -8.564  21.627 41.901 1.000 44.932  ? 612 HOH   AAA O   1 ? 
HETATM 4370 O  O   . HOH   I 5 .   ? -27.619 26.656 27.087 1.000 50.764  ? 613 HOH   AAA O   1 ? 
HETATM 4371 O  O   . HOH   I 5 .   ? 5.757   30.257 53.298 1.000 37.423  ? 614 HOH   AAA O   1 ? 
HETATM 4372 O  O   . HOH   I 5 .   ? -1.754  24.265 21.906 1.000 38.667  ? 615 HOH   AAA O   1 ? 
HETATM 4373 O  O   . HOH   I 5 .   ? -27.985 31.550 26.589 1.000 38.017  ? 616 HOH   AAA O   1 ? 
HETATM 4374 O  O   . HOH   I 5 .   ? -21.905 21.205 56.575 1.000 49.360  ? 617 HOH   AAA O   1 ? 
HETATM 4375 O  O   . HOH   I 5 .   ? -29.906 21.847 40.811 1.000 38.690  ? 618 HOH   AAA O   1 ? 
HETATM 4376 O  O   . HOH   I 5 .   ? -30.744 24.325 41.515 1.000 32.172  ? 619 HOH   AAA O   1 ? 
HETATM 4377 O  O   . HOH   J 5 .   ? 27.400  57.988 59.453 0.500 27.313  ? 401 HOH   BBB O   1 ? 
HETATM 4378 O  O   . HOH   J 5 .   ? 42.347  34.405 53.672 0.500 37.844  ? 402 HOH   BBB O   1 ? 
HETATM 4379 O  O   . HOH   J 5 .   ? 11.222  25.231 67.675 1.000 54.322  ? 403 HOH   BBB O   1 ? 
HETATM 4380 O  O   . HOH   J 5 .   ? 48.319  38.429 54.272 0.500 40.696  ? 404 HOH   BBB O   1 ? 
HETATM 4381 O  O   . HOH   J 5 .   ? 16.909  48.685 73.387 1.000 40.464  ? 405 HOH   BBB O   1 ? 
HETATM 4382 O  O   . HOH   J 5 .   ? 32.136  40.287 81.954 0.500 20.510  ? 406 HOH   BBB O   1 ? 
HETATM 4383 O  O   . HOH   J 5 .   ? 5.934   33.191 59.462 1.000 36.022  ? 407 HOH   BBB O   1 ? 
HETATM 4384 O  O   . HOH   J 5 .   ? 21.749  40.558 79.344 0.500 34.777  ? 408 HOH   BBB O   1 ? 
HETATM 4385 O  O   . HOH   J 5 .   ? 26.296  45.156 47.345 1.000 28.191  ? 409 HOH   BBB O   1 ? 
HETATM 4386 O  O   . HOH   J 5 .   ? 9.878   40.532 50.135 1.000 38.692  ? 410 HOH   BBB O   1 ? 
HETATM 4387 O  O   . HOH   J 5 .   ? 28.457  20.168 47.706 1.000 36.992  ? 411 HOH   BBB O   1 ? 
HETATM 4388 O  O   . HOH   J 5 .   ? 7.184   50.020 61.611 1.000 52.657  ? 412 HOH   BBB O   1 ? 
HETATM 4389 O  O   . HOH   J 5 .   ? 45.727  42.885 51.583 1.000 60.983  ? 413 HOH   BBB O   1 ? 
HETATM 4390 O  O   . HOH   J 5 .   ? 34.475  47.429 75.523 1.000 35.060  ? 414 HOH   BBB O   1 ? 
HETATM 4391 O  O   . HOH   J 5 .   ? 16.345  47.590 42.712 1.000 34.329  ? 415 HOH   BBB O   1 ? 
HETATM 4392 O  O   . HOH   J 5 .   ? 18.547  28.214 78.080 1.000 46.654  ? 416 HOH   BBB O   1 ? 
HETATM 4393 O  O   . HOH   J 5 .   ? 38.918  42.665 74.514 1.000 43.399  ? 417 HOH   BBB O   1 ? 
HETATM 4394 O  O   . HOH   J 5 .   ? 23.752  28.929 56.471 1.000 22.690  ? 418 HOH   BBB O   1 ? 
HETATM 4395 O  O   . HOH   J 5 .   ? 36.653  31.003 48.547 1.000 34.493  ? 419 HOH   BBB O   1 ? 
HETATM 4396 O  O   . HOH   J 5 .   ? 11.604  25.694 60.076 1.000 39.762  ? 420 HOH   BBB O   1 ? 
HETATM 4397 O  O   . HOH   J 5 .   ? 28.434  40.800 79.894 1.000 28.348  ? 421 HOH   BBB O   1 ? 
HETATM 4398 O  O   . HOH   J 5 .   ? 44.871  46.146 67.026 1.000 48.958  ? 422 HOH   BBB O   1 ? 
HETATM 4399 O  O   . HOH   J 5 .   ? 12.625  44.719 38.163 1.000 43.619  ? 423 HOH   BBB O   1 ? 
HETATM 4400 O  O   . HOH   J 5 .   ? 21.493  21.653 74.409 1.000 48.247  ? 424 HOH   BBB O   1 ? 
HETATM 4401 O  O   . HOH   J 5 .   ? 18.938  25.885 45.438 1.000 48.266  ? 425 HOH   BBB O   1 ? 
HETATM 4402 O  O   . HOH   J 5 .   ? 28.604  32.888 84.231 1.000 51.842  ? 426 HOH   BBB O   1 ? 
HETATM 4403 O  O   . HOH   J 5 .   ? 1.854   38.804 64.133 1.000 30.739  ? 427 HOH   BBB O   1 ? 
HETATM 4404 O  O   . HOH   J 5 .   ? 9.307   45.567 50.750 1.000 27.339  ? 428 HOH   BBB O   1 ? 
HETATM 4405 O  O   . HOH   J 5 .   ? 24.708  34.316 45.228 1.000 38.451  ? 429 HOH   BBB O   1 ? 
HETATM 4406 O  O   . HOH   J 5 .   ? 8.011   33.074 70.381 1.000 33.452  ? 430 HOH   BBB O   1 ? 
HETATM 4407 O  O   . HOH   J 5 .   ? 6.134   29.237 41.393 1.000 44.389  ? 431 HOH   BBB O   1 ? 
HETATM 4408 O  O   . HOH   J 5 .   ? 20.467  25.485 63.269 1.000 28.476  ? 432 HOH   BBB O   1 ? 
HETATM 4409 O  O   . HOH   J 5 .   ? 31.992  49.977 57.303 1.000 28.869  ? 433 HOH   BBB O   1 ? 
HETATM 4410 O  O   . HOH   J 5 .   ? 26.364  53.035 66.636 1.000 44.377  ? 434 HOH   BBB O   1 ? 
HETATM 4411 O  O   . HOH   J 5 .   ? 15.334  48.369 59.401 1.000 38.367  ? 435 HOH   BBB O   1 ? 
HETATM 4412 O  O   . HOH   J 5 .   ? 15.434  42.512 73.024 1.000 33.601  ? 436 HOH   BBB O   1 ? 
HETATM 4413 O  O   . HOH   J 5 .   ? 26.944  54.810 50.964 1.000 43.395  ? 437 HOH   BBB O   1 ? 
HETATM 4414 O  O   . HOH   J 5 .   ? 22.589  23.524 79.704 1.000 34.115  ? 438 HOH   BBB O   1 ? 
HETATM 4415 O  O   . HOH   J 5 .   ? 24.743  20.986 72.666 1.000 40.672  ? 439 HOH   BBB O   1 ? 
HETATM 4416 O  O   . HOH   J 5 .   ? 33.037  56.925 62.086 1.000 33.920  ? 440 HOH   BBB O   1 ? 
HETATM 4417 O  O   . HOH   J 5 .   ? 24.571  53.784 48.049 1.000 35.997  ? 441 HOH   BBB O   1 ? 
HETATM 4418 O  O   . HOH   J 5 .   ? 10.965  29.286 66.898 1.000 43.534  ? 442 HOH   BBB O   1 ? 
HETATM 4419 O  O   . HOH   J 5 .   ? 33.350  50.494 68.468 1.000 42.509  ? 443 HOH   BBB O   1 ? 
HETATM 4420 O  O   . HOH   J 5 .   ? 27.612  55.319 67.412 1.000 53.587  ? 444 HOH   BBB O   1 ? 
HETATM 4421 O  O   . HOH   J 5 .   ? 12.430  29.475 38.253 1.000 30.099  ? 445 HOH   BBB O   1 ? 
HETATM 4422 O  O   . HOH   J 5 .   ? 8.646   35.518 32.019 1.000 35.178  ? 446 HOH   BBB O   1 ? 
HETATM 4423 O  O   . HOH   J 5 .   ? 21.732  34.489 54.962 1.000 20.202  ? 447 HOH   BBB O   1 ? 
HETATM 4424 O  O   . HOH   J 5 .   ? 28.021  47.063 47.968 1.000 41.520  ? 448 HOH   BBB O   1 ? 
HETATM 4425 O  O   . HOH   J 5 .   ? 15.918  34.666 74.384 1.000 47.966  ? 449 HOH   BBB O   1 ? 
HETATM 4426 O  O   . HOH   J 5 .   ? 32.434  18.546 62.025 1.000 37.317  ? 450 HOH   BBB O   1 ? 
HETATM 4427 O  O   . HOH   J 5 .   ? 10.382  27.884 47.440 1.000 29.816  ? 451 HOH   BBB O   1 ? 
HETATM 4428 O  O   . HOH   J 5 .   ? 16.596  38.118 34.088 1.000 42.711  ? 452 HOH   BBB O   1 ? 
HETATM 4429 O  O   . HOH   J 5 .   ? 38.294  35.655 63.975 1.000 27.680  ? 453 HOH   BBB O   1 ? 
HETATM 4430 O  O   . HOH   J 5 .   ? 17.758  25.173 55.732 1.000 31.051  ? 454 HOH   BBB O   1 ? 
HETATM 4431 O  O   . HOH   J 5 .   ? 39.037  22.069 60.942 1.000 31.431  ? 455 HOH   BBB O   1 ? 
HETATM 4432 O  O   . HOH   J 5 .   ? 17.907  31.746 74.784 1.000 45.806  ? 456 HOH   BBB O   1 ? 
HETATM 4433 O  O   . HOH   J 5 .   ? 26.515  21.949 68.333 1.000 25.503  ? 457 HOH   BBB O   1 ? 
HETATM 4434 O  O   . HOH   J 5 .   ? 16.618  50.337 63.043 1.000 39.553  ? 458 HOH   BBB O   1 ? 
HETATM 4435 O  O   . HOH   J 5 .   ? 37.596  21.775 67.483 1.000 34.287  ? 459 HOH   BBB O   1 ? 
HETATM 4436 O  O   . HOH   J 5 .   ? 37.316  53.178 67.652 1.000 69.907  ? 460 HOH   BBB O   1 ? 
HETATM 4437 O  O   . HOH   J 5 .   ? 22.704  40.204 74.840 1.000 24.532  ? 461 HOH   BBB O   1 ? 
HETATM 4438 O  O   . HOH   J 5 .   ? 11.494  31.119 60.322 1.000 21.510  ? 462 HOH   BBB O   1 ? 
HETATM 4439 O  O   . HOH   J 5 .   ? 30.038  43.512 51.991 1.000 40.964  ? 463 HOH   BBB O   1 ? 
HETATM 4440 O  O   . HOH   J 5 .   ? 16.963  50.476 49.934 1.000 34.860  ? 464 HOH   BBB O   1 ? 
HETATM 4441 O  O   . HOH   J 5 .   ? 12.256  44.213 42.884 1.000 25.815  ? 465 HOH   BBB O   1 ? 
HETATM 4442 O  O   . HOH   J 5 .   ? 25.319  45.589 77.412 1.000 46.787  ? 466 HOH   BBB O   1 ? 
HETATM 4443 O  O   . HOH   J 5 .   ? 16.834  39.321 38.820 1.000 24.366  ? 467 HOH   BBB O   1 ? 
HETATM 4444 O  O   . HOH   J 5 .   ? 30.638  19.780 60.603 1.000 36.643  ? 468 HOH   BBB O   1 ? 
HETATM 4445 O  O   . HOH   J 5 .   ? 32.236  41.365 79.652 1.000 32.401  ? 469 HOH   BBB O   1 ? 
HETATM 4446 O  O   . HOH   J 5 .   ? 6.946   36.742 46.437 1.000 29.177  ? 470 HOH   BBB O   1 ? 
HETATM 4447 O  O   . HOH   J 5 .   ? 20.486  36.570 70.704 1.000 18.998  ? 471 HOH   BBB O   1 ? 
HETATM 4448 O  O   . HOH   J 5 .   ? 19.143  38.145 54.910 1.000 20.049  ? 472 HOH   BBB O   1 ? 
HETATM 4449 O  O   . HOH   J 5 .   ? 34.623  23.030 44.961 1.000 34.258  ? 473 HOH   BBB O   1 ? 
HETATM 4450 O  O   . HOH   J 5 .   ? 27.570  24.196 73.895 1.000 31.794  ? 474 HOH   BBB O   1 ? 
HETATM 4451 O  O   . HOH   J 5 .   ? 16.133  37.754 75.718 1.000 29.261  ? 475 HOH   BBB O   1 ? 
HETATM 4452 O  O   . HOH   J 5 .   ? 37.608  29.276 63.972 1.000 30.244  ? 476 HOH   BBB O   1 ? 
HETATM 4453 O  O   . HOH   J 5 .   ? 16.394  31.769 37.841 1.000 34.330  ? 477 HOH   BBB O   1 ? 
HETATM 4454 O  O   . HOH   J 5 .   ? 12.863  46.167 68.546 1.000 45.369  ? 478 HOH   BBB O   1 ? 
HETATM 4455 O  O   . HOH   J 5 .   ? 38.965  31.320 64.739 1.000 31.673  ? 479 HOH   BBB O   1 ? 
HETATM 4456 O  O   . HOH   J 5 .   ? 36.455  26.083 51.903 1.000 35.296  ? 480 HOH   BBB O   1 ? 
HETATM 4457 O  O   . HOH   J 5 .   ? 26.149  30.895 80.009 1.000 31.880  ? 481 HOH   BBB O   1 ? 
HETATM 4458 O  O   . HOH   J 5 .   ? 38.121  32.736 67.042 1.000 31.635  ? 482 HOH   BBB O   1 ? 
HETATM 4459 O  O   . HOH   J 5 .   ? 26.883  40.600 49.419 1.000 23.736  ? 483 HOH   BBB O   1 ? 
HETATM 4460 O  O   . HOH   J 5 .   ? 41.130  40.693 76.899 1.000 52.170  ? 484 HOH   BBB O   1 ? 
HETATM 4461 O  O   . HOH   J 5 .   ? 27.248  36.568 53.701 1.000 38.204  ? 485 HOH   BBB O   1 ? 
HETATM 4462 O  O   . HOH   J 5 .   ? 7.529   46.490 54.360 1.000 32.966  ? 486 HOH   BBB O   1 ? 
HETATM 4463 O  O   . HOH   J 5 .   ? 39.612  37.339 75.900 1.000 47.362  ? 487 HOH   BBB O   1 ? 
HETATM 4464 O  O   . HOH   J 5 .   ? 30.885  45.763 51.742 1.000 39.541  ? 488 HOH   BBB O   1 ? 
HETATM 4465 O  O   . HOH   J 5 .   ? 17.263  28.408 75.583 1.000 30.431  ? 489 HOH   BBB O   1 ? 
HETATM 4466 O  O   . HOH   J 5 .   ? 3.963   39.668 55.262 1.000 23.793  ? 490 HOH   BBB O   1 ? 
HETATM 4467 O  O   . HOH   J 5 .   ? 25.950  51.622 68.736 1.000 33.477  ? 491 HOH   BBB O   1 ? 
HETATM 4468 O  O   . HOH   J 5 .   ? 3.824   37.231 65.216 1.000 24.783  ? 492 HOH   BBB O   1 ? 
HETATM 4469 O  O   . HOH   J 5 .   ? 5.117   42.480 57.842 1.000 28.928  ? 493 HOH   BBB O   1 ? 
HETATM 4470 O  O   . HOH   J 5 .   ? 41.049  21.298 62.719 1.000 52.680  ? 494 HOH   BBB O   1 ? 
HETATM 4471 O  O   . HOH   J 5 .   ? 8.212   44.294 44.349 1.000 35.169  ? 495 HOH   BBB O   1 ? 
HETATM 4472 O  O   . HOH   J 5 .   ? 34.270  39.150 81.457 1.000 26.432  ? 496 HOH   BBB O   1 ? 
HETATM 4473 O  O   . HOH   J 5 .   ? 7.512   48.260 44.773 1.000 40.199  ? 497 HOH   BBB O   1 ? 
HETATM 4474 O  O   . HOH   J 5 .   ? 36.319  24.170 48.140 1.000 32.334  ? 498 HOH   BBB O   1 ? 
HETATM 4475 O  O   . HOH   J 5 .   ? 26.506  56.295 65.228 1.000 65.418  ? 499 HOH   BBB O   1 ? 
HETATM 4476 O  O   . HOH   J 5 .   ? 9.445   38.030 70.698 1.000 29.069  ? 500 HOH   BBB O   1 ? 
HETATM 4477 O  O   . HOH   J 5 .   ? 16.952  52.791 47.292 1.000 32.751  ? 501 HOH   BBB O   1 ? 
HETATM 4478 O  O   . HOH   J 5 .   ? 34.122  52.894 55.094 1.000 36.643  ? 502 HOH   BBB O   1 ? 
HETATM 4479 O  O   . HOH   J 5 .   ? 32.942  21.671 63.744 1.000 31.798  ? 503 HOH   BBB O   1 ? 
HETATM 4480 O  O   . HOH   J 5 .   ? 15.922  44.828 67.189 1.000 29.055  ? 504 HOH   BBB O   1 ? 
HETATM 4481 O  O   . HOH   J 5 .   ? 31.792  17.138 69.140 1.000 43.058  ? 505 HOH   BBB O   1 ? 
HETATM 4482 O  O   . HOH   J 5 .   ? 24.451  20.287 67.633 1.000 35.439  ? 506 HOH   BBB O   1 ? 
HETATM 4483 O  O   . HOH   J 5 .   ? 15.681  29.339 42.258 1.000 39.962  ? 507 HOH   BBB O   1 ? 
HETATM 4484 O  O   . HOH   J 5 .   ? 12.402  41.314 39.462 1.000 28.115  ? 508 HOH   BBB O   1 ? 
HETATM 4485 O  O   . HOH   J 5 .   ? 32.976  18.864 72.329 1.000 50.718  ? 509 HOH   BBB O   1 ? 
HETATM 4486 O  O   . HOH   J 5 .   ? 6.851   45.759 57.011 1.000 44.897  ? 510 HOH   BBB O   1 ? 
HETATM 4487 O  O   . HOH   J 5 .   ? 3.039   41.840 61.905 1.000 34.388  ? 511 HOH   BBB O   1 ? 
HETATM 4488 O  O   . HOH   J 5 .   ? 37.334  26.735 71.982 1.000 32.034  ? 512 HOH   BBB O   1 ? 
HETATM 4489 O  O   . HOH   J 5 .   ? 24.304  35.122 53.877 1.000 21.059  ? 513 HOH   BBB O   1 ? 
HETATM 4490 O  O   . HOH   J 5 .   ? 29.221  43.304 76.101 1.000 25.156  ? 514 HOH   BBB O   1 ? 
HETATM 4491 O  O   . HOH   J 5 .   ? 5.217   46.293 67.528 1.000 34.342  ? 515 HOH   BBB O   1 ? 
HETATM 4492 O  O   . HOH   J 5 .   ? 17.307  30.486 50.598 1.000 36.715  ? 516 HOH   BBB O   1 ? 
HETATM 4493 O  O   . HOH   J 5 .   ? 6.950   40.028 71.374 1.000 44.230  ? 517 HOH   BBB O   1 ? 
HETATM 4494 O  O   . HOH   J 5 .   ? 13.585  51.259 52.894 1.000 29.424  ? 518 HOH   BBB O   1 ? 
HETATM 4495 O  O   . HOH   J 5 .   ? 33.787  51.715 58.147 1.000 32.501  ? 519 HOH   BBB O   1 ? 
HETATM 4496 O  O   . HOH   J 5 .   ? 38.040  44.523 51.471 1.000 45.121  ? 520 HOH   BBB O   1 ? 
HETATM 4497 O  O   . HOH   J 5 .   ? 24.771  55.953 53.778 1.000 31.087  ? 521 HOH   BBB O   1 ? 
HETATM 4498 O  O   . HOH   J 5 .   ? 19.627  33.261 76.002 1.000 38.667  ? 522 HOH   BBB O   1 ? 
HETATM 4499 O  O   . HOH   J 5 .   ? 27.966  18.407 53.843 1.000 43.889  ? 523 HOH   BBB O   1 ? 
HETATM 4500 O  O   . HOH   J 5 .   ? 20.910  22.399 68.037 1.000 34.392  ? 524 HOH   BBB O   1 ? 
HETATM 4501 O  O   . HOH   J 5 .   ? 26.537  21.339 56.679 1.000 33.886  ? 525 HOH   BBB O   1 ? 
HETATM 4502 O  O   . HOH   J 5 .   ? 2.905   43.088 66.382 1.000 40.229  ? 526 HOH   BBB O   1 ? 
HETATM 4503 O  O   . HOH   J 5 .   ? 8.004   28.447 53.984 1.000 41.232  ? 527 HOH   BBB O   1 ? 
HETATM 4504 O  O   . HOH   J 5 .   ? 38.544  24.188 74.129 1.000 44.259  ? 528 HOH   BBB O   1 ? 
HETATM 4505 O  O   . HOH   J 5 .   ? 35.774  30.507 73.085 1.000 35.185  ? 529 HOH   BBB O   1 ? 
HETATM 4506 O  O   . HOH   J 5 .   ? 35.765  32.868 71.244 1.000 24.884  ? 530 HOH   BBB O   1 ? 
HETATM 4507 O  O   . HOH   J 5 .   ? 15.307  49.099 48.203 1.000 38.948  ? 531 HOH   BBB O   1 ? 
HETATM 4508 O  O   . HOH   J 5 .   ? 39.237  45.333 70.453 1.000 31.435  ? 532 HOH   BBB O   1 ? 
HETATM 4509 O  O   . HOH   J 5 .   ? 16.508  46.224 69.367 1.000 31.851  ? 533 HOH   BBB O   1 ? 
HETATM 4510 O  O   . HOH   J 5 .   ? 14.674  35.014 32.794 1.000 44.924  ? 534 HOH   BBB O   1 ? 
HETATM 4511 O  O   . HOH   J 5 .   ? 23.324  38.697 43.489 1.000 37.215  ? 535 HOH   BBB O   1 ? 
HETATM 4512 O  O   . HOH   J 5 .   ? 39.074  27.555 56.764 0.500 19.788  ? 536 HOH   BBB O   1 ? 
HETATM 4513 O  O   . HOH   J 5 .   ? 22.745  50.681 44.699 1.000 56.487  ? 537 HOH   BBB O   1 ? 
HETATM 4514 O  O   . HOH   J 5 .   ? 22.374  49.559 70.375 1.000 48.666  ? 538 HOH   BBB O   1 ? 
HETATM 4515 O  O   . HOH   J 5 .   ? 5.790   34.443 52.522 1.000 22.223  ? 539 HOH   BBB O   1 ? 
HETATM 4516 O  O   . HOH   J 5 .   ? 29.948  41.116 82.349 1.000 32.348  ? 540 HOH   BBB O   1 ? 
HETATM 4517 O  O   . HOH   J 5 .   ? 21.142  19.420 52.493 1.000 42.948  ? 541 HOH   BBB O   1 ? 
HETATM 4518 O  O   . HOH   J 5 .   ? 7.478   45.866 59.594 1.000 34.800  ? 542 HOH   BBB O   1 ? 
HETATM 4519 O  O   . HOH   J 5 .   ? 14.490  29.138 47.024 1.000 34.441  ? 543 HOH   BBB O   1 ? 
HETATM 4520 O  O   . HOH   J 5 .   ? 39.921  36.213 73.421 1.000 47.536  ? 544 HOH   BBB O   1 ? 
HETATM 4521 O  O   . HOH   J 5 .   ? 44.814  31.379 59.967 1.000 39.275  ? 545 HOH   BBB O   1 ? 
HETATM 4522 O  O   . HOH   J 5 .   ? 18.106  26.568 47.996 1.000 45.764  ? 546 HOH   BBB O   1 ? 
HETATM 4523 O  O   . HOH   J 5 .   ? 29.604  33.225 50.185 1.000 41.242  ? 547 HOH   BBB O   1 ? 
HETATM 4524 O  O   . HOH   J 5 .   ? 21.945  32.174 53.607 1.000 20.258  ? 548 HOH   BBB O   1 ? 
HETATM 4525 O  O   . HOH   J 5 .   ? 6.653   33.039 50.307 1.000 24.470  ? 549 HOH   BBB O   1 ? 
HETATM 4526 O  O   . HOH   J 5 .   ? 21.799  44.840 39.554 1.000 47.493  ? 550 HOH   BBB O   1 ? 
HETATM 4527 O  O   . HOH   J 5 .   ? 46.561  46.141 57.543 1.000 55.580  ? 551 HOH   BBB O   1 ? 
HETATM 4528 O  O   . HOH   J 5 .   ? 12.952  24.747 69.876 1.000 36.775  ? 552 HOH   BBB O   1 ? 
HETATM 4529 O  O   . HOH   J 5 .   ? 18.093  54.048 51.595 1.000 34.274  ? 553 HOH   BBB O   1 ? 
HETATM 4530 O  O   . HOH   J 5 .   ? 13.622  27.758 49.485 1.000 42.822  ? 554 HOH   BBB O   1 ? 
HETATM 4531 O  O   . HOH   J 5 .   ? 31.237  25.166 76.140 1.000 26.605  ? 555 HOH   BBB O   1 ? 
HETATM 4532 O  O   . HOH   J 5 .   ? 39.737  28.428 57.327 0.500 35.830  ? 556 HOH   BBB O   1 ? 
HETATM 4533 O  O   . HOH   J 5 .   ? 11.289  31.877 68.371 1.000 36.932  ? 557 HOH   BBB O   1 ? 
HETATM 4534 O  O   . HOH   J 5 .   ? 14.170  50.975 60.286 1.000 40.630  ? 558 HOH   BBB O   1 ? 
HETATM 4535 O  O   . HOH   J 5 .   ? 19.722  54.015 61.721 1.000 33.339  ? 559 HOH   BBB O   1 ? 
HETATM 4536 O  O   . HOH   J 5 .   ? 32.267  39.636 84.272 1.000 34.133  ? 560 HOH   BBB O   1 ? 
HETATM 4537 O  O   . HOH   J 5 .   ? 11.472  29.269 34.993 1.000 57.188  ? 561 HOH   BBB O   1 ? 
HETATM 4538 O  O   . HOH   J 5 .   ? 42.435  47.284 79.264 1.000 41.402  ? 562 HOH   BBB O   1 ? 
HETATM 4539 O  O   . HOH   J 5 .   ? 28.590  25.430 75.687 1.000 30.930  ? 563 HOH   BBB O   1 ? 
HETATM 4540 O  O   . HOH   J 5 .   ? 12.879  43.465 70.058 1.000 28.706  ? 564 HOH   BBB O   1 ? 
HETATM 4541 O  O   . HOH   J 5 .   ? 20.113  22.575 64.227 1.000 40.017  ? 565 HOH   BBB O   1 ? 
HETATM 4542 O  O   . HOH   J 5 .   ? 27.221  32.133 82.089 1.000 40.037  ? 566 HOH   BBB O   1 ? 
HETATM 4543 O  O   . HOH   J 5 .   ? 5.787   32.540 54.655 1.000 24.917  ? 567 HOH   BBB O   1 ? 
HETATM 4544 O  O   . HOH   J 5 .   ? 18.481  42.978 76.238 1.000 31.641  ? 568 HOH   BBB O   1 ? 
HETATM 4545 O  O   . HOH   J 5 .   ? 19.142  45.838 40.244 1.000 31.949  ? 569 HOH   BBB O   1 ? 
HETATM 4546 O  O   . HOH   J 5 .   ? 16.525  43.833 74.522 0.500 36.744  ? 570 HOH   BBB O   1 ? 
HETATM 4547 O  O   . HOH   J 5 .   ? 8.351   42.641 51.064 1.000 36.885  ? 571 HOH   BBB O   1 ? 
HETATM 4548 O  O   . HOH   J 5 .   ? 36.462  23.325 51.638 1.000 33.583  ? 572 HOH   BBB O   1 ? 
HETATM 4549 O  O   . HOH   J 5 .   ? 26.451  21.947 47.323 1.000 47.003  ? 573 HOH   BBB O   1 ? 
HETATM 4550 O  O   . HOH   J 5 .   ? 38.966  34.768 70.653 1.000 51.108  ? 574 HOH   BBB O   1 ? 
HETATM 4551 O  O   . HOH   J 5 .   ? 41.890  40.475 68.172 1.000 46.897  ? 575 HOH   BBB O   1 ? 
HETATM 4552 O  O   . HOH   J 5 .   ? 14.094  25.415 57.795 1.000 52.195  ? 576 HOH   BBB O   1 ? 
HETATM 4553 O  O   . HOH   J 5 .   ? 28.550  18.654 69.561 1.000 44.927  ? 577 HOH   BBB O   1 ? 
HETATM 4554 O  O   . HOH   J 5 .   ? 5.814   40.870 51.058 1.000 55.358  ? 578 HOH   BBB O   1 ? 
HETATM 4555 O  O   . HOH   J 5 .   ? 32.901  25.342 43.936 1.000 36.265  ? 579 HOH   BBB O   1 ? 
HETATM 4556 O  O   . HOH   J 5 .   ? 28.380  35.698 51.271 1.000 35.572  ? 580 HOH   BBB O   1 ? 
HETATM 4557 O  O   . HOH   J 5 .   ? 42.389  41.790 47.688 1.000 51.090  ? 581 HOH   BBB O   1 ? 
HETATM 4558 O  O   . HOH   J 5 .   ? 19.075  50.375 69.671 1.000 43.896  ? 582 HOH   BBB O   1 ? 
HETATM 4559 O  O   . HOH   J 5 .   ? 19.828  42.495 38.182 1.000 57.101  ? 583 HOH   BBB O   1 ? 
HETATM 4560 O  O   . HOH   J 5 .   ? 21.315  24.637 81.963 1.000 55.279  ? 584 HOH   BBB O   1 ? 
HETATM 4561 O  O   . HOH   J 5 .   ? 8.919   51.775 62.262 1.000 37.965  ? 585 HOH   BBB O   1 ? 
HETATM 4562 O  O   . HOH   J 5 .   ? 6.263   39.268 45.864 1.000 35.002  ? 586 HOH   BBB O   1 ? 
HETATM 4563 O  O   . HOH   J 5 .   ? 26.675  34.642 49.176 1.000 46.485  ? 587 HOH   BBB O   1 ? 
HETATM 4564 O  O   . HOH   J 5 .   ? 29.344  41.080 49.786 1.000 46.352  ? 588 HOH   BBB O   1 ? 
HETATM 4565 O  O   . HOH   J 5 .   ? 12.088  38.851 71.989 1.000 44.919  ? 589 HOH   BBB O   1 ? 
HETATM 4566 O  O   . HOH   J 5 .   ? 45.465  30.866 57.342 1.000 51.587  ? 590 HOH   BBB O   1 ? 
HETATM 4567 O  O   . HOH   J 5 .   ? 26.188  18.309 66.371 1.000 60.579  ? 591 HOH   BBB O   1 ? 
HETATM 4568 O  O   . HOH   J 5 .   ? 27.655  43.055 46.245 1.000 24.963  ? 592 HOH   BBB O   1 ? 
HETATM 4569 O  O   . HOH   J 5 .   ? 15.951  52.067 51.657 1.000 41.003  ? 593 HOH   BBB O   1 ? 
HETATM 4570 O  O   . HOH   J 5 .   ? 4.225   43.469 60.282 1.000 38.298  ? 594 HOH   BBB O   1 ? 
HETATM 4571 O  O   . HOH   J 5 .   ? 37.909  29.105 72.644 1.000 42.887  ? 595 HOH   BBB O   1 ? 
HETATM 4572 O  O   . HOH   J 5 .   ? 29.904  42.455 78.676 1.000 31.704  ? 596 HOH   BBB O   1 ? 
HETATM 4573 O  O   . HOH   J 5 .   ? 6.455   47.361 63.079 1.000 37.744  ? 597 HOH   BBB O   1 ? 
HETATM 4574 O  O   . HOH   J 5 .   ? 38.080  43.229 49.369 1.000 38.429  ? 598 HOH   BBB O   1 ? 
HETATM 4575 O  O   . HOH   J 5 .   ? 37.967  32.539 69.611 1.000 31.274  ? 599 HOH   BBB O   1 ? 
HETATM 4576 O  O   . HOH   J 5 .   ? 23.549  36.881 41.689 1.000 45.321  ? 600 HOH   BBB O   1 ? 
HETATM 4577 O  O   . HOH   J 5 .   ? 10.659  42.910 40.917 1.000 27.223  ? 601 HOH   BBB O   1 ? 
HETATM 4578 O  O   . HOH   J 5 .   ? 6.560   30.411 50.849 1.000 32.471  ? 602 HOH   BBB O   1 ? 
HETATM 4579 O  O   . HOH   J 5 .   ? 23.358  19.755 70.039 1.000 42.302  ? 603 HOH   BBB O   1 ? 
HETATM 4580 O  O   . HOH   J 5 .   ? 9.894   45.343 39.286 1.000 54.373  ? 604 HOH   BBB O   1 ? 
HETATM 4581 O  O   . HOH   J 5 .   ? 3.025   42.254 56.105 1.000 23.828  ? 605 HOH   BBB O   1 ? 
HETATM 4582 O  O   . HOH   J 5 .   ? 18.967  31.327 37.531 1.000 44.802  ? 606 HOH   BBB O   1 ? 
HETATM 4583 O  O   . HOH   J 5 .   ? 5.457   38.150 72.682 0.500 39.354  ? 607 HOH   BBB O   1 ? 
HETATM 4584 O  O   . HOH   J 5 .   ? 23.534  31.141 80.744 1.000 47.644  ? 608 HOH   BBB O   1 ? 
HETATM 4585 O  O   . HOH   J 5 .   ? 36.571  26.742 49.211 1.000 46.290  ? 609 HOH   BBB O   1 ? 
HETATM 4586 O  O   . HOH   J 5 .   ? 4.243   46.450 56.603 1.000 51.554  ? 610 HOH   BBB O   1 ? 
HETATM 4587 O  O   . HOH   J 5 .   ? 15.044  29.607 39.368 1.000 38.932  ? 611 HOH   BBB O   1 ? 
HETATM 4588 O  O   . HOH   J 5 .   ? 17.690  41.412 37.297 1.000 36.979  ? 612 HOH   BBB O   1 ? 
HETATM 4589 O  O   . HOH   J 5 .   ? 42.768  49.639 79.829 1.000 55.487  ? 613 HOH   BBB O   1 ? 
HETATM 4590 O  O   . HOH   J 5 .   ? 15.214  51.319 46.285 1.000 41.369  ? 614 HOH   BBB O   1 ? 
HETATM 4591 O  O   . HOH   J 5 .   ? 35.253  58.426 62.048 1.000 36.312  ? 615 HOH   BBB O   1 ? 
HETATM 4592 O  O   . HOH   J 5 .   ? 41.078  30.214 66.373 1.000 40.723  ? 616 HOH   BBB O   1 ? 
HETATM 4593 O  O   . HOH   J 5 .   ? 14.956  44.650 71.202 1.000 36.720  ? 617 HOH   BBB O   1 ? 
HETATM 4594 O  O   . HOH   J 5 .   ? 39.127  25.410 70.473 1.000 45.552  ? 618 HOH   BBB O   1 ? 
HETATM 4595 O  O   . HOH   J 5 .   ? 36.581  47.651 79.925 1.000 39.703  ? 619 HOH   BBB O   1 ? 
HETATM 4596 O  O   . HOH   J 5 .   ? 39.733  30.488 70.687 1.000 31.013  ? 620 HOH   BBB O   1 ? 
HETATM 4597 O  O   . HOH   J 5 .   ? 40.681  29.002 68.397 1.000 44.271  ? 621 HOH   BBB O   1 ? 
HETATM 4598 O  O   . HOH   J 5 .   ? 35.674  60.120 59.684 1.000 42.617  ? 622 HOH   BBB O   1 ? 
HETATM 4599 O  O   . HOH   J 5 .   ? 23.261  56.224 47.208 1.000 50.596  ? 623 HOH   BBB O   1 ? 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . ASP   A 5   ? 1.181 0.669 0.879 -0.006 0.276  -0.108 4   ASP   AAA N   
2    C  CA  . ASP   A 5   ? 0.889 0.596 0.656 0.191  0.211  0.103  4   ASP   AAA CA  
3    C  C   . ASP   A 5   ? 0.757 0.439 0.617 0.166  -0.023 0.068  4   ASP   AAA C   
4    O  O   . ASP   A 5   ? 1.080 0.410 0.849 0.293  0.168  -0.009 4   ASP   AAA O   
5    C  CB  . ASP   A 5   ? 0.884 0.745 0.619 0.071  0.224  0.066  4   ASP   AAA CB  
6    C  CG  . ASP   A 5   ? 0.945 0.735 0.736 0.285  0.104  0.195  4   ASP   AAA CG  
7    O  OD1 . ASP   A 5   ? 0.839 1.100 0.869 0.223  -0.094 -0.007 4   ASP   AAA OD1 
8    O  OD2 . ASP   A 5   ? 1.099 0.563 1.779 0.193  0.074  -0.421 4   ASP   AAA OD2 
9    N  N   . TRP   A 6   ? 0.595 0.215 0.577 0.164  0.050  0.029  5   TRP   AAA N   
10   C  CA  . TRP   A 6   ? 0.515 0.150 0.540 -0.003 0.026  -0.006 5   TRP   AAA CA  
11   C  C   . TRP   A 6   ? 0.506 0.141 0.444 0.022  -0.015 0.011  5   TRP   AAA C   
12   O  O   . TRP   A 6   ? 0.497 0.127 0.470 0.055  0.005  -0.010 5   TRP   AAA O   
13   C  CB  . TRP   A 6   ? 0.550 0.035 0.549 0.101  0.060  -0.060 5   TRP   AAA CB  
14   C  CG  . TRP   A 6   ? 0.478 0.013 0.574 0.035  0.036  0.049  5   TRP   AAA CG  
15   C  CD1 . TRP   A 6   ? 0.519 0.049 0.510 0.026  0.074  0.064  5   TRP   AAA CD1 
16   C  CD2 . TRP   A 6   ? 0.414 0.031 0.435 0.085  0.033  -0.001 5   TRP   AAA CD2 
17   N  NE1 . TRP   A 6   ? 0.448 0.008 0.518 0.026  0.070  -0.009 5   TRP   AAA NE1 
18   C  CE2 . TRP   A 6   ? 0.364 0.010 0.495 0.001  0.046  0.043  5   TRP   AAA CE2 
19   C  CE3 . TRP   A 6   ? 0.421 0.087 0.474 0.050  0.058  0.016  5   TRP   AAA CE3 
20   C  CZ2 . TRP   A 6   ? 0.415 0.012 0.546 -0.048 0.052  -0.012 5   TRP   AAA CZ2 
21   C  CZ3 . TRP   A 6   ? 0.347 0.027 0.469 0.077  0.043  -0.014 5   TRP   AAA CZ3 
22   C  CH2 . TRP   A 6   ? 0.377 0.010 0.493 -0.035 0.041  0.002  5   TRP   AAA CH2 
23   N  N   . GLY   A 7   ? 0.434 0.165 0.513 0.016  0.017  0.039  6   GLY   AAA N   
24   C  CA  . GLY   A 7   ? 0.437 0.127 0.509 0.037  0.040  0.070  6   GLY   AAA CA  
25   C  C   . GLY   A 7   ? 0.447 0.141 0.463 0.018  -0.015 0.071  6   GLY   AAA C   
26   O  O   . GLY   A 7   ? 0.426 0.137 0.518 0.048  -0.026 0.022  6   GLY   AAA O   
27   N  N   . TYR   A 8   ? 0.468 0.128 0.520 0.002  -0.007 0.051  7   TYR   AAA N   
28   C  CA  . TYR   A 8   ? 0.456 0.015 0.631 0.052  0.010  0.038  7   TYR   AAA CA  
29   C  C   . TYR   A 8   ? 0.524 0.214 0.649 0.177  -0.096 0.111  7   TYR   AAA C   
30   O  O   . TYR   A 8   ? 0.758 0.151 0.699 0.161  0.046  0.098  7   TYR   AAA O   
31   C  CB  . TYR   A 8   ? 0.395 0.093 0.491 -0.033 -0.054 0.054  7   TYR   AAA CB  
32   C  CG  . TYR   A 8   ? 0.425 0.007 0.526 0.004  0.016  0.019  7   TYR   AAA CG  
33   C  CD1 . TYR   A 8   ? 0.435 0.009 0.560 -0.028 0.010  -0.016 7   TYR   AAA CD1 
34   C  CD2 . TYR   A 8   ? 0.332 0.041 0.452 0.024  -0.037 -0.038 7   TYR   AAA CD2 
35   C  CE1 . TYR   A 8   ? 0.339 0.051 0.445 -0.011 0.030  -0.048 7   TYR   AAA CE1 
36   C  CE2 . TYR   A 8   ? 0.337 0.010 0.438 0.005  -0.002 -0.037 7   TYR   AAA CE2 
37   C  CZ  . TYR   A 8   ? 0.286 0.056 0.430 0.041  -0.018 -0.039 7   TYR   AAA CZ  
38   O  OH  . TYR   A 8   ? 0.293 0.034 0.429 0.011  0.001  0.000  7   TYR   AAA OH  
39   N  N   . ASP   A 9   ? 0.455 0.068 0.653 0.089  -0.004 0.111  8   ASP   AAA N   
40   C  CA  . ASP   A 9   ? 0.522 0.186 0.663 0.161  -0.024 0.147  8   ASP   AAA CA  
41   C  C   . ASP   A 9   ? 0.575 0.204 0.781 0.100  0.114  0.091  8   ASP   AAA C   
42   O  O   . ASP   A 9   ? 0.649 0.200 0.570 0.110  0.076  0.029  8   ASP   AAA O   
43   C  CB  . ASP   A 9   ? 0.687 0.208 0.805 0.016  -0.124 -0.037 8   ASP   AAA CB  
44   C  CG  . ASP   A 9   ? 0.950 0.619 0.808 0.094  -0.015 -0.014 8   ASP   AAA CG  
45   O  OD1 . ASP   A 9   ? 1.094 0.670 0.871 0.068  -0.173 0.157  8   ASP   AAA OD1 
46   O  OD2 . ASP   A 9   ? 1.093 0.831 1.036 0.332  -0.138 -0.316 8   ASP   AAA OD2 
47   N  N   . ASP   A 10  ? 0.733 0.339 0.819 0.226  0.100  0.236  9   ASP   AAA N   
48   C  CA  . ASP   A 10  ? 0.701 0.499 0.815 0.203  0.152  -0.032 9   ASP   AAA CA  
49   C  C   . ASP   A 10  ? 0.645 0.370 0.705 0.201  0.126  0.026  9   ASP   AAA C   
50   O  O   . ASP   A 10  ? 1.006 0.544 0.754 -0.170 0.149  -0.073 9   ASP   AAA O   
51   C  CB  . ASP   A 10  ? 0.877 0.537 0.964 0.230  0.156  0.334  9   ASP   AAA CB  
52   C  CG  . ASP   A 10  ? 0.788 0.779 1.068 0.249  0.101  0.209  9   ASP   AAA CG  
53   O  OD1 . ASP   A 10  ? 0.971 0.694 1.107 0.260  0.383  0.206  9   ASP   AAA OD1 
54   O  OD2 . ASP   A 10  ? 0.775 0.642 1.139 0.004  -0.116 0.054  9   ASP   AAA OD2 
55   N  N   . LYS   A 11  ? 0.675 0.356 0.659 0.123  0.097  0.067  10  LYS   AAA N   
56   C  CA  . LYS   A 11  ? 0.674 0.274 0.757 0.066  0.027  0.166  10  LYS   AAA CA  
57   C  C   . LYS   A 11  ? 0.726 0.196 0.712 0.054  0.053  0.171  10  LYS   AAA C   
58   O  O   . LYS   A 11  ? 0.810 0.250 1.080 0.114  0.008  0.208  10  LYS   AAA O   
59   C  CB  . LYS   A 11  ? 0.822 0.555 0.786 0.164  0.015  0.030  10  LYS   AAA CB  
60   C  CG  . LYS   A 11  ? 0.749 0.436 0.994 0.167  0.054  -0.020 10  LYS   AAA CG  
61   C  CD  . LYS   A 11  ? 0.934 0.236 0.750 -0.045 -0.077 -0.121 10  LYS   AAA CD  
62   C  CE  . LYS   A 11  ? 0.799 0.492 0.724 -0.049 -0.169 -0.034 10  LYS   AAA CE  
63   N  NZ  . LYS   A 11  ? 0.609 0.060 0.712 -0.025 -0.069 -0.009 10  LYS   AAA NZ  
64   N  N   . ASN   A 12  ? 0.680 0.164 0.724 0.148  0.009  0.138  11  ASN   AAA N   
65   C  CA  . ASN   A 12  ? 0.623 0.197 0.577 0.110  0.028  0.062  11  ASN   AAA CA  
66   C  C   . ASN   A 12  ? 0.432 0.192 0.584 0.114  0.026  0.110  11  ASN   AAA C   
67   O  O   . ASN   A 12  ? 0.461 0.113 0.576 0.100  -0.008 0.039  11  ASN   AAA O   
68   C  CB  . ASN   A 12  ? 0.604 0.267 0.556 0.126  -0.020 0.041  11  ASN   AAA CB  
69   C  CG  . ASN   A 12  ? 0.604 0.417 0.508 0.090  0.020  0.062  11  ASN   AAA CG  
70   O  OD1 . ASN   A 12  ? 0.482 0.213 0.567 0.070  0.044  0.135  11  ASN   AAA OD1 
71   N  ND2 . ASN   A 12  ? 0.522 0.180 0.591 -0.006 0.005  0.137  11  ASN   AAA ND2 
72   N  N   . GLY   A 13  ? 0.582 0.065 0.585 0.010  0.075  0.093  12  GLY   AAA N   
73   C  CA  . GLY   A 13  ? 0.464 0.020 0.563 0.019  0.019  0.022  12  GLY   AAA CA  
74   C  C   . GLY   A 13  ? 0.362 0.110 0.432 0.057  0.090  -0.059 12  GLY   AAA C   
75   O  O   . GLY   A 13  ? 0.572 0.038 0.719 -0.044 0.123  0.067  12  GLY   AAA O   
76   N  N   . PRO   A 14  ? 0.402 0.121 0.479 0.038  0.093  -0.092 13  PRO   AAA N   
77   C  CA  . PRO   A 14  ? 0.410 0.193 0.560 -0.021 0.057  -0.052 13  PRO   AAA CA  
78   C  C   . PRO   A 14  ? 0.470 0.142 0.630 0.016  0.080  0.044  13  PRO   AAA C   
79   O  O   . PRO   A 14  ? 0.487 0.040 0.666 0.038  0.088  0.012  13  PRO   AAA O   
80   C  CB  . PRO   A 14  ? 0.419 0.279 0.615 -0.025 0.096  -0.005 13  PRO   AAA CB  
81   C  CG  . PRO   A 14  ? 0.462 0.082 0.606 0.091  0.088  -0.061 13  PRO   AAA CG  
82   C  CD  . PRO   A 14  ? 0.459 0.268 0.529 0.040  0.180  -0.014 13  PRO   AAA CD  
83   N  N   . GLU   A 15  ? 0.585 0.015 0.871 -0.071 0.112  -0.004 14  GLU   AAA N   
84   C  CA  . GLU   A 15  ? 0.633 0.096 0.818 -0.228 0.047  -0.061 14  GLU   AAA CA  
85   C  C   . GLU   A 15  ? 0.619 0.075 0.810 0.075  0.062  0.071  14  GLU   AAA C   
86   O  O   . GLU   A 15  ? 0.832 0.321 0.803 -0.060 -0.003 -0.032 14  GLU   AAA O   
87   C  CB  . GLU   A 15  ? 0.847 0.303 0.962 0.018  0.205  0.004  14  GLU   AAA CB  
88   C  CG  . GLU   A 15  ? 1.021 0.275 0.921 0.021  0.211  0.087  14  GLU   AAA CG  
89   C  CD  . GLU   A 15  ? 1.180 1.102 0.861 0.067  0.190  -0.010 14  GLU   AAA CD  
90   O  OE1 . GLU   A 15  ? 1.175 0.717 0.937 0.025  0.151  -0.247 14  GLU   AAA OE1 
91   O  OE2 . GLU   A 15  ? 1.069 0.279 1.359 -0.257 0.380  0.063  14  GLU   AAA OE2 
92   N  N   . GLN   A 16  ? 0.630 0.091 0.848 0.065  0.024  0.051  15  GLN   AAA N   
93   C  CA  . GLN   A 16  ? 0.709 0.210 0.855 -0.006 0.029  0.059  15  GLN   AAA CA  
94   C  C   . GLN   A 16  ? 0.725 0.325 0.541 0.039  0.103  0.114  15  GLN   AAA C   
95   O  O   . GLN   A 16  ? 0.586 0.131 0.586 -0.050 0.038  0.107  15  GLN   AAA O   
96   C  CB  . GLN   A 16  ? 0.825 0.336 0.872 0.052  -0.020 0.122  15  GLN   AAA CB  
97   C  CG  . GLN   A 16  ? 0.949 0.604 1.126 0.191  0.007  -0.005 15  GLN   AAA CG  
98   C  CD  . GLN   A 16  ? 0.993 0.658 1.289 0.336  0.134  -0.092 15  GLN   AAA CD  
99   O  OE1 . GLN   A 16  ? 0.949 1.124 1.405 0.350  0.011  0.550  15  GLN   AAA OE1 
100  N  NE2 . GLN   A 16  ? 0.949 0.049 1.631 0.090  -0.057 -0.125 15  GLN   AAA NE2 
101  N  N   . TRP   A 17  ? 0.459 0.218 0.567 0.059  0.103  0.088  16  TRP   AAA N   
102  C  CA  . TRP   A 17  ? 0.434 0.162 0.452 0.008  0.080  0.041  16  TRP   AAA CA  
103  C  C   . TRP   A 17  ? 0.420 0.145 0.464 0.011  0.073  0.014  16  TRP   AAA C   
104  O  O   . TRP   A 17  ? 0.488 0.076 0.477 -0.006 0.095  0.026  16  TRP   AAA O   
105  C  CB  . TRP   A 17  ? 0.420 0.118 0.436 0.038  0.108  0.020  16  TRP   AAA CB  
106  C  CG  . TRP   A 17  ? 0.404 0.076 0.393 0.054  0.076  0.074  16  TRP   AAA CG  
107  C  CD1 . TRP   A 17  ? 0.424 0.104 0.407 -0.010 0.055  0.109  16  TRP   AAA CD1 
108  C  CD2 . TRP   A 17  ? 0.413 0.010 0.480 0.033  0.109  0.023  16  TRP   AAA CD2 
109  N  NE1 . TRP   A 17  ? 0.399 0.055 0.436 0.016  0.027  0.017  16  TRP   AAA NE1 
110  C  CE2 . TRP   A 17  ? 0.431 0.030 0.432 0.030  0.088  0.031  16  TRP   AAA CE2 
111  C  CE3 . TRP   A 17  ? 0.405 0.009 0.464 -0.009 0.157  0.026  16  TRP   AAA CE3 
112  C  CZ2 . TRP   A 17  ? 0.374 0.009 0.465 0.032  0.038  -0.007 16  TRP   AAA CZ2 
113  C  CZ3 . TRP   A 17  ? 0.440 0.014 0.480 0.044  0.054  0.042  16  TRP   AAA CZ3 
114  C  CH2 . TRP   A 17  ? 0.429 0.022 0.490 0.081  0.041  0.015  16  TRP   AAA CH2 
115  N  N   . SER   A 18  ? 0.480 0.122 0.533 0.030  0.081  -0.027 17  SER   AAA N   
116  C  CA  . SER   A 18  ? 0.477 0.155 0.566 0.060  0.058  -0.003 17  SER   AAA CA  
117  C  C   . SER   A 18  ? 0.571 0.046 0.506 0.016  0.057  -0.058 17  SER   AAA C   
118  O  O   . SER   A 18  ? 0.557 0.196 0.628 -0.014 0.018  -0.075 17  SER   AAA O   
119  C  CB  . SER   A 18  ? 0.531 0.300 0.540 0.043  0.055  -0.050 17  SER   AAA CB  
120  O  OG  . SER   A 18  ? 0.604 0.129 0.596 -0.005 0.078  0.035  17  SER   AAA OG  
121  N  N   . LYS   A 19  ? 0.571 0.025 0.522 -0.085 0.079  -0.021 18  LYS   AAA N   
122  C  CA  . LYS   A 19  ? 0.627 0.092 0.540 -0.032 0.139  -0.061 18  LYS   AAA CA  
123  C  C   . LYS   A 19  ? 0.727 0.059 0.661 0.021  0.127  -0.006 18  LYS   AAA C   
124  O  O   . LYS   A 19  ? 0.794 0.010 0.770 0.044  0.155  0.042  18  LYS   AAA O   
125  C  CB  . LYS   A 19  ? 0.693 0.142 0.616 -0.002 0.167  0.035  18  LYS   AAA CB  
126  C  CG  . LYS   A 19  ? 0.621 0.471 0.821 0.157  0.270  -0.015 18  LYS   AAA CG  
127  C  CD  . LYS   A 19  ? 0.696 0.746 0.874 0.123  0.250  0.122  18  LYS   AAA CD  
128  C  CE  . LYS   A 19  ? 0.703 0.841 0.965 0.179  0.343  0.114  18  LYS   AAA CE  
129  N  NZ  . LYS   A 19  ? 0.781 1.242 0.860 0.168  0.314  -0.049 18  LYS   AAA NZ  
130  N  N   . LEU   A 20  ? 0.666 0.046 0.643 0.034  0.157  0.159  19  LEU   AAA N   
131  C  CA  . LEU   A 20  ? 0.722 0.247 0.482 0.065  0.123  -0.011 19  LEU   AAA CA  
132  C  C   . LEU   A 20  ? 0.586 0.144 0.593 -0.052 0.123  0.047  19  LEU   AAA C   
133  O  O   . LEU   A 20  ? 0.605 0.208 0.533 -0.051 0.084  0.002  19  LEU   AAA O   
134  C  CB  . LEU   A 20  ? 0.782 0.215 0.677 0.118  0.076  -0.129 19  LEU   AAA CB  
135  C  CG  . LEU   A 20  ? 1.067 0.661 0.613 0.047  0.192  -0.005 19  LEU   AAA CG  
136  C  CD1 . LEU   A 20  ? 1.054 0.668 0.684 0.186  -0.099 -0.029 19  LEU   AAA CD1 
137  C  CD2 . LEU   A 20  ? 0.992 0.555 0.631 0.424  0.257  0.052  19  LEU   AAA CD2 
138  N  N   . TYR   A 21  ? 0.635 0.011 0.637 -0.040 0.165  -0.050 20  TYR   AAA N   
139  C  CA  . TYR   A 21  ? 0.482 0.088 0.515 -0.073 0.140  -0.016 20  TYR   AAA CA  
140  C  C   . TYR   A 21  ? 0.510 0.043 0.642 0.052  0.030  -0.036 20  TYR   AAA C   
141  O  O   . TYR   A 21  ? 0.541 0.053 0.650 -0.069 0.124  -0.048 20  TYR   AAA O   
142  C  CB  . TYR   A 21  ? 0.458 0.025 0.506 -0.037 0.105  0.005  20  TYR   AAA CB  
143  C  CG  . TYR   A 21  ? 0.443 0.052 0.460 -0.005 0.091  0.029  20  TYR   AAA CG  
144  C  CD1 . TYR   A 21  ? 0.432 0.124 0.552 0.000  0.120  -0.025 20  TYR   AAA CD1 
145  C  CD2 . TYR   A 21  ? 0.476 0.060 0.542 0.057  0.051  0.076  20  TYR   AAA CD2 
146  C  CE1 . TYR   A 21  ? 0.530 0.125 0.540 0.019  0.074  -0.027 20  TYR   AAA CE1 
147  C  CE2 . TYR   A 21  ? 0.511 0.274 0.489 -0.015 0.094  0.069  20  TYR   AAA CE2 
148  C  CZ  . TYR   A 21  ? 0.512 0.175 0.513 -0.068 0.069  -0.025 20  TYR   AAA CZ  
149  O  OH  . TYR   A 21  ? 0.716 0.175 0.544 -0.194 0.194  -0.083 20  TYR   AAA OH  
150  N  N   . PRO   A 22  ? 0.514 0.064 0.607 0.003  0.066  -0.150 21  PRO   AAA N   
151  C  CA  . PRO   A 22  ? 0.618 0.025 0.506 -0.030 0.138  -0.097 21  PRO   AAA CA  
152  C  C   . PRO   A 22  ? 0.525 0.014 0.506 -0.060 0.116  -0.029 21  PRO   AAA C   
153  O  O   . PRO   A 22  ? 0.579 0.015 0.610 0.004  0.029  -0.071 21  PRO   AAA O   
154  C  CB  . PRO   A 22  ? 0.673 0.037 0.634 -0.102 0.151  -0.094 21  PRO   AAA CB  
155  C  CG  . PRO   A 22  ? 0.539 0.065 0.676 -0.160 0.161  -0.103 21  PRO   AAA CG  
156  C  CD  . PRO   A 22  ? 0.621 0.016 0.679 -0.060 0.124  -0.061 21  PRO   AAA CD  
157  N  N   . ILE   A 23  ? 0.508 0.034 0.579 -0.076 0.109  -0.110 22  ILE   AAA N   
158  C  CA  . ILE   A 23  ? 0.398 0.010 0.631 -0.006 0.061  -0.045 22  ILE   AAA CA  
159  C  C   . ILE   A 23  ? 0.434 0.019 0.477 -0.012 0.028  -0.078 22  ILE   AAA C   
160  O  O   . ILE   A 23  ? 0.456 0.081 0.533 -0.007 0.058  -0.050 22  ILE   AAA O   
161  C  CB  . ILE   A 23  ? 0.411 0.013 0.586 -0.014 0.077  -0.060 22  ILE   AAA CB  
162  C  CG1 . ILE   A 23  ? 0.406 0.111 0.606 -0.017 0.026  -0.040 22  ILE   AAA CG1 
163  C  CG2 . ILE   A 23  ? 0.397 0.108 0.555 -0.004 0.023  -0.047 22  ILE   AAA CG2 
164  C  CD1 . ILE   A 23  ? 0.413 0.278 0.542 -0.040 0.021  -0.041 22  ILE   AAA CD1 
165  N  N   . ALA   A 24  ? 0.408 0.058 0.548 -0.062 0.032  -0.098 23  ALA   AAA N   
166  C  CA  . ALA   A 24  ? 0.473 0.020 0.530 -0.066 0.087  -0.026 23  ALA   AAA CA  
167  C  C   . ALA   A 24  ? 0.418 0.075 0.455 -0.028 0.090  -0.038 23  ALA   AAA C   
168  O  O   . ALA   A 24  ? 0.499 0.010 0.577 0.022  0.167  -0.017 23  ALA   AAA O   
169  C  CB  . ALA   A 24  ? 0.443 0.030 0.505 -0.052 0.067  -0.099 23  ALA   AAA CB  
170  N  N   . ASN   A 25  ? 0.457 0.170 0.514 -0.134 0.065  -0.046 24  ASN   AAA N   
171  C  CA  . ASN   A 25  ? 0.575 0.090 0.587 -0.019 0.047  -0.029 24  ASN   AAA CA  
172  C  C   . ASN   A 25  ? 0.548 0.127 0.542 -0.005 0.048  -0.061 24  ASN   AAA C   
173  O  O   . ASN   A 25  ? 0.541 0.152 0.662 -0.061 0.074  -0.118 24  ASN   AAA O   
174  C  CB  . ASN   A 25  ? 0.616 0.115 0.549 -0.054 0.033  -0.045 24  ASN   AAA CB  
175  C  CG  . ASN   A 25  ? 0.579 0.169 0.572 -0.112 0.007  -0.134 24  ASN   AAA CG  
176  O  OD1 . ASN   A 25  ? 0.812 0.199 0.735 0.030  -0.039 -0.067 24  ASN   AAA OD1 
177  N  ND2 . ASN   A 25  ? 0.529 0.223 0.638 0.027  0.109  0.044  24  ASN   AAA ND2 
178  N  N   . GLY   A 26  ? 0.502 0.072 0.689 -0.076 0.095  -0.030 25  GLY   AAA N   
179  C  CA  . GLY   A 26  ? 0.531 0.013 0.680 -0.058 0.065  -0.026 25  GLY   AAA CA  
180  C  C   . GLY   A 26  ? 0.516 0.073 0.676 -0.173 0.026  -0.081 25  GLY   AAA C   
181  O  O   . GLY   A 26  ? 0.468 0.114 0.607 -0.153 0.035  -0.075 25  GLY   AAA O   
182  N  N   . ASN   A 27  ? 0.439 0.073 0.585 -0.155 0.047  -0.097 26  ASN   AAA N   
183  C  CA  . ASN   A 27  ? 0.490 0.132 0.588 -0.151 0.080  -0.128 26  ASN   AAA CA  
184  C  C   . ASN   A 27  ? 0.397 0.184 0.483 -0.147 0.075  -0.114 26  ASN   AAA C   
185  O  O   . ASN   A 27  ? 0.425 0.220 0.492 -0.124 0.051  -0.119 26  ASN   AAA O   
186  C  CB  . ASN   A 27  ? 0.475 0.331 0.588 -0.154 0.101  -0.116 26  ASN   AAA CB  
187  C  CG  . ASN   A 27  ? 0.582 0.364 0.649 -0.155 0.177  -0.061 26  ASN   AAA CG  
188  O  OD1 . ASN   A 27  ? 0.664 0.390 0.642 -0.097 0.151  -0.126 26  ASN   AAA OD1 
189  N  ND2 . ASN   A 27  ? 0.600 0.560 0.634 -0.273 0.187  -0.174 26  ASN   AAA ND2 
190  N  N   . ASN   A 28  ? 0.391 0.101 0.519 -0.056 0.024  -0.102 27  ASN   AAA N   
191  C  CA  . ASN   A 28  ? 0.344 0.177 0.481 -0.091 0.032  -0.075 27  ASN   AAA CA  
192  C  C   . ASN   A 28  ? 0.349 0.036 0.501 -0.089 0.036  -0.065 27  ASN   AAA C   
193  O  O   . ASN   A 28  ? 0.409 0.033 0.482 -0.089 0.051  -0.069 27  ASN   AAA O   
194  C  CB  . ASN   A 28  ? 0.393 0.051 0.531 -0.109 0.051  -0.099 27  ASN   AAA CB  
195  C  CG  . ASN   A 28  ? 0.338 0.247 0.444 -0.012 0.042  -0.050 27  ASN   AAA CG  
196  O  OD1 . ASN   A 28  ? 0.498 0.361 0.471 0.069  0.023  -0.027 27  ASN   AAA OD1 
197  N  ND2 . ASN   A 28  ? 0.355 0.093 0.601 -0.042 0.048  -0.098 27  ASN   AAA ND2 
198  N  N   . GLN   A 29  ? 0.385 0.044 0.517 -0.025 0.035  -0.092 28  GLN   AAA N   
199  C  CA  . GLN   A 29  ? 0.371 0.155 0.417 -0.001 0.042  -0.056 28  GLN   AAA CA  
200  C  C   . GLN   A 29  ? 0.317 0.051 0.365 -0.002 -0.000 -0.052 28  GLN   AAA C   
201  O  O   . GLN   A 29  ? 0.383 0.067 0.413 -0.075 0.003  -0.089 28  GLN   AAA O   
202  C  CB  . GLN   A 29  ? 0.370 0.128 0.435 -0.004 0.050  -0.059 28  GLN   AAA CB  
203  C  CG  . GLN   A 29  ? 0.392 0.123 0.449 -0.053 0.050  -0.111 28  GLN   AAA CG  
204  C  CD  . GLN   A 29  ? 0.317 0.062 0.432 -0.040 0.042  -0.056 28  GLN   AAA CD  
205  O  OE1 . GLN   A 29  ? 0.357 0.032 0.482 -0.075 0.028  -0.044 28  GLN   AAA OE1 
206  N  NE2 . GLN   A 29  ? 0.335 0.020 0.507 -0.033 0.080  -0.016 28  GLN   AAA NE2 
207  N  N   . SER   A 30  ? 0.336 0.025 0.429 0.017  0.009  -0.087 29  SER   AAA N   
208  C  CA  . SER   A 30  ? 0.418 0.016 0.460 -0.018 0.026  -0.065 29  SER   AAA CA  
209  C  C   . SER   A 30  ? 0.440 0.026 0.549 0.009  0.004  -0.104 29  SER   AAA C   
210  O  O   . SER   A 30  ? 0.374 0.042 0.509 -0.001 0.019  -0.026 29  SER   AAA O   
211  C  CB  . SER   A 30  ? 0.357 0.018 0.408 -0.001 0.030  -0.069 29  SER   AAA CB  
212  O  OG  . SER   A 30  ? 0.308 0.012 0.428 -0.030 0.015  -0.036 29  SER   AAA OG  
213  N  N   . PRO   A 31  ? 0.472 0.021 0.505 -0.006 0.043  -0.086 30  PRO   AAA N   
214  C  CA  . PRO   A 31  ? 0.370 0.014 0.493 0.032  0.008  -0.048 30  PRO   AAA CA  
215  C  C   . PRO   A 31  ? 0.323 0.049 0.372 -0.094 0.087  -0.097 30  PRO   AAA C   
216  O  O   . PRO   A 31  ? 0.362 0.018 0.489 -0.037 0.035  -0.066 30  PRO   AAA O   
217  C  CB  . PRO   A 31  ? 0.340 0.071 0.369 0.008  0.032  -0.027 30  PRO   AAA CB  
218  C  CG  . PRO   A 31  ? 0.369 0.010 0.460 -0.020 0.011  -0.036 30  PRO   AAA CG  
219  C  CD  . PRO   A 31  ? 0.456 0.014 0.510 -0.046 0.065  -0.045 30  PRO   AAA CD  
220  N  N   . VAL   A 32  ? 0.328 0.043 0.377 -0.061 0.071  -0.070 31  VAL   AAA N   
221  C  CA  . VAL   A 32  ? 0.373 0.020 0.490 -0.034 0.077  -0.076 31  VAL   AAA CA  
222  C  C   . VAL   A 32  ? 0.334 0.039 0.447 -0.034 0.061  -0.118 31  VAL   AAA C   
223  O  O   . VAL   A 32  ? 0.355 0.020 0.462 -0.032 0.022  -0.072 31  VAL   AAA O   
224  C  CB  . VAL   A 32  ? 0.364 0.032 0.507 0.006  0.055  -0.111 31  VAL   AAA CB  
225  C  CG1 . VAL   A 32  ? 0.343 0.019 0.539 0.011  0.040  -0.052 31  VAL   AAA CG1 
226  C  CG2 . VAL   A 32  ? 0.337 0.041 0.456 0.023  0.047  -0.011 31  VAL   AAA CG2 
227  N  N   . ASP   A 33  ? 0.353 0.017 0.484 0.008  0.033  -0.069 32  ASP   AAA N   
228  C  CA  . ASP   A 33  ? 0.393 0.015 0.508 -0.053 0.062  -0.038 32  ASP   AAA CA  
229  C  C   . ASP   A 33  ? 0.376 0.018 0.484 -0.061 0.056  -0.037 32  ASP   AAA C   
230  O  O   . ASP   A 33  ? 0.395 0.119 0.568 -0.035 0.037  -0.052 32  ASP   AAA O   
231  C  CB  . ASP   A 33  ? 0.420 0.010 0.515 -0.000 0.075  -0.044 32  ASP   AAA CB  
232  C  CG  . ASP   A 33  ? 0.415 0.099 0.455 -0.033 0.049  -0.121 32  ASP   AAA CG  
233  O  OD1 . ASP   A 33  ? 0.368 0.095 0.482 0.004  0.029  -0.065 32  ASP   AAA OD1 
234  O  OD2 . ASP   A 33  ? 0.530 0.036 0.514 -0.043 0.084  -0.121 32  ASP   AAA OD2 
235  N  N   . ILE   A 34  ? 0.361 0.027 0.482 -0.067 0.034  -0.068 33  ILE   AAA N   
236  C  CA  . ILE   A 34  ? 0.353 0.036 0.466 -0.058 0.037  -0.101 33  ILE   AAA CA  
237  C  C   . ILE   A 34  ? 0.355 0.135 0.440 -0.076 0.040  -0.113 33  ILE   AAA C   
238  O  O   . ILE   A 34  ? 0.387 0.045 0.535 -0.089 0.049  -0.109 33  ILE   AAA O   
239  C  CB  . ILE   A 34  ? 0.378 0.024 0.440 -0.063 0.046  -0.031 33  ILE   AAA CB  
240  C  CG1 . ILE   A 34  ? 0.345 0.013 0.449 -0.031 0.025  -0.044 33  ILE   AAA CG1 
241  C  CG2 . ILE   A 34  ? 0.387 0.053 0.460 -0.024 0.033  -0.032 33  ILE   AAA CG2 
242  C  CD1 . ILE   A 34  ? 0.428 0.024 0.511 0.008  0.017  -0.095 33  ILE   AAA CD1 
243  N  N   . LYS   A 35  ? 0.355 0.110 0.522 -0.035 0.017  -0.147 34  LYS   AAA N   
244  C  CA  . LYS   A 35  ? 0.398 0.105 0.474 -0.039 0.030  -0.099 34  LYS   AAA CA  
245  C  C   . LYS   A 35  ? 0.376 0.185 0.452 -0.017 0.026  -0.100 34  LYS   AAA C   
246  O  O   . LYS   A 35  ? 0.409 0.272 0.472 0.104  -0.021 -0.143 34  LYS   AAA O   
247  C  CB  . LYS   A 35  ? 0.471 0.158 0.505 -0.131 0.011  -0.096 34  LYS   AAA CB  
248  C  CG  . LYS   A 35  ? 0.567 0.133 0.574 -0.004 0.065  -0.033 34  LYS   AAA CG  
249  C  CD  . LYS   A 35  ? 0.824 0.149 0.686 -0.123 0.064  -0.035 34  LYS   AAA CD  
250  C  CE  . LYS   A 35  ? 0.854 0.335 0.696 0.014  0.090  -0.025 34  LYS   AAA CE  
251  N  NZ  . LYS   A 35  ? 0.682 0.337 0.679 -0.070 0.143  0.000  34  LYS   AAA NZ  
252  N  N   . THR   A 36  ? 0.379 0.112 0.458 -0.008 0.043  -0.130 35  THR   AAA N   
253  C  CA  . THR   A 36  ? 0.427 0.208 0.428 -0.027 0.042  -0.063 35  THR   AAA CA  
254  C  C   . THR   A 36  ? 0.440 0.170 0.435 -0.086 0.043  -0.019 35  THR   AAA C   
255  O  O   . THR   A 36  ? 0.612 0.099 0.568 -0.058 -0.035 -0.033 35  THR   AAA O   
256  C  CB  . THR   A 36  ? 0.365 0.285 0.474 -0.021 0.023  -0.123 35  THR   AAA CB  
257  O  OG1 . THR   A 36  ? 0.422 0.126 0.514 -0.028 0.050  -0.100 35  THR   AAA OG1 
258  C  CG2 . THR   A 36  ? 0.466 0.251 0.572 0.027  -0.066 -0.173 35  THR   AAA CG2 
259  N  N   . SER   A 37  ? 0.562 0.229 0.483 -0.029 -0.002 -0.152 36  SER   AAA N   
260  C  CA  . SER   A 37  ? 0.477 0.333 0.493 -0.058 0.028  -0.156 36  SER   AAA CA  
261  C  C   . SER   A 37  ? 0.451 0.281 0.472 -0.070 0.023  -0.206 36  SER   AAA C   
262  O  O   . SER   A 37  ? 0.450 0.669 0.509 0.024  -0.009 -0.286 36  SER   AAA O   
263  C  CB  . SER   A 37  ? 0.615 0.269 0.492 -0.058 0.037  -0.145 36  SER   AAA CB  
264  O  OG  . SER   A 37  ? 0.647 0.387 0.525 -0.138 0.037  -0.072 36  SER   AAA OG  
265  N  N   . GLU   A 38  ? 0.449 0.251 0.444 -0.128 0.011  -0.127 37  GLU   AAA N   
266  C  CA  . GLU   A 38  ? 0.400 0.362 0.485 -0.072 -0.011 -0.132 37  GLU   AAA CA  
267  C  C   . GLU   A 38  ? 0.426 0.288 0.538 -0.150 -0.025 -0.139 37  GLU   AAA C   
268  O  O   . GLU   A 38  ? 0.471 0.226 0.615 -0.171 0.049  -0.143 37  GLU   AAA O   
269  C  CB  . GLU   A 38  ? 0.555 0.119 0.588 -0.156 0.038  -0.150 37  GLU   AAA CB  
270  C  CG  . GLU   A 38  ? 0.564 0.352 0.651 0.066  0.071  -0.116 37  GLU   AAA CG  
271  C  CD  . GLU   A 38  ? 0.794 0.367 0.798 -0.192 -0.022 -0.077 37  GLU   AAA CD  
272  O  OE1 . GLU   A 38  ? 1.076 0.286 0.902 0.024  0.102  -0.056 37  GLU   AAA OE1 
273  O  OE2 . GLU   A 38  ? 1.095 0.647 1.045 -0.026 -0.200 -0.402 37  GLU   AAA OE2 
274  N  N   . THR   A 39  ? 0.459 0.229 0.506 -0.103 -0.002 -0.124 38  THR   AAA N   
275  C  CA  . THR   A 39  ? 0.421 0.324 0.499 -0.088 0.010  -0.187 38  THR   AAA CA  
276  C  C   . THR   A 39  ? 0.416 0.475 0.488 -0.116 0.016  -0.188 38  THR   AAA C   
277  O  O   . THR   A 39  ? 0.471 0.433 0.498 -0.083 0.046  -0.177 38  THR   AAA O   
278  C  CB  . THR   A 39  ? 0.426 0.301 0.439 -0.107 0.029  -0.145 38  THR   AAA CB  
279  O  OG1 . THR   A 39  ? 0.432 0.293 0.409 -0.072 0.024  -0.085 38  THR   AAA OG1 
280  C  CG2 . THR   A 39  ? 0.412 0.218 0.483 -0.094 0.032  -0.124 38  THR   AAA CG2 
281  N  N   . LYS   A 40  ? 0.563 0.215 0.495 -0.077 -0.022 -0.146 39  LYS   AAA N   
282  C  CA  . LYS   A 40  ? 0.586 0.208 0.559 -0.093 -0.030 -0.088 39  LYS   AAA CA  
283  C  C   . LYS   A 40  ? 0.559 0.204 0.528 -0.132 0.045  -0.096 39  LYS   AAA C   
284  O  O   . LYS   A 40  ? 0.480 0.341 0.546 0.081  -0.039 -0.116 39  LYS   AAA O   
285  C  CB  . LYS   A 40  ? 0.599 0.466 0.627 -0.152 0.005  -0.060 39  LYS   AAA CB  
286  C  CG  . LYS   A 40  ? 0.898 0.453 0.910 -0.298 -0.030 0.052  39  LYS   AAA CG  
287  C  CD  . LYS   A 40  ? 1.022 0.445 0.911 -0.459 -0.121 0.128  39  LYS   AAA CD  
288  C  CE  . LYS   A 40  ? 1.242 0.456 0.936 -0.585 -0.077 -0.037 39  LYS   AAA CE  
289  N  NZ  . LYS   A 40  ? 1.108 0.522 1.172 -0.362 -0.124 -0.231 39  LYS   AAA NZ  
290  N  N   . HIS   A 41  ? 0.538 0.167 0.492 -0.020 0.005  -0.088 40  HIS   AAA N   
291  C  CA  . HIS   A 41  ? 0.607 0.164 0.619 -0.070 -0.053 -0.085 40  HIS   AAA CA  
292  C  C   . HIS   A 41  ? 0.588 0.403 0.552 -0.064 -0.059 -0.106 40  HIS   AAA C   
293  O  O   . HIS   A 41  ? 0.517 0.663 0.619 -0.020 -0.097 -0.228 40  HIS   AAA O   
294  C  CB  . HIS   A 41  ? 0.591 0.363 0.604 -0.051 -0.037 -0.063 40  HIS   AAA CB  
295  C  CG  . HIS   A 41  ? 0.676 0.430 0.503 -0.058 -0.156 0.063  40  HIS   AAA CG  
296  N  ND1 . HIS   A 41  ? 0.678 0.624 0.624 -0.049 -0.180 -0.063 40  HIS   AAA ND1 
297  C  CD2 . HIS   A 41  ? 0.657 0.545 0.585 -0.068 -0.230 0.084  40  HIS   AAA CD2 
298  C  CE1 . HIS   A 41  ? 0.668 0.616 0.587 -0.034 -0.177 -0.066 40  HIS   AAA CE1 
299  N  NE2 . HIS   A 41  ? 0.863 0.570 0.595 -0.012 -0.257 0.021  40  HIS   AAA NE2 
300  N  N   . ASP   A 42  ? 0.580 0.579 0.516 0.053  -0.115 -0.157 41  ASP   AAA N   
301  C  CA  . ASP   A 42  ? 0.606 0.541 0.499 0.080  -0.089 -0.155 41  ASP   AAA CA  
302  C  C   . ASP   A 42  ? 0.690 0.561 0.509 0.046  -0.185 -0.071 41  ASP   AAA C   
303  O  O   . ASP   A 42  ? 0.595 0.569 0.551 0.050  -0.075 -0.145 41  ASP   AAA O   
304  C  CB  . ASP   A 42  ? 0.542 0.557 0.506 -0.009 -0.110 -0.139 41  ASP   AAA CB  
305  C  CG  . ASP   A 42  ? 0.506 0.618 0.414 -0.024 -0.069 -0.110 41  ASP   AAA CG  
306  O  OD1 . ASP   A 42  ? 0.645 0.659 0.563 -0.013 -0.120 -0.010 41  ASP   AAA OD1 
307  O  OD2 . ASP   A 42  ? 0.521 0.676 0.521 -0.006 -0.014 -0.005 41  ASP   AAA OD2 
308  N  N   . THR   A 43  ? 0.809 0.450 0.504 0.208  -0.173 -0.036 42  THR   AAA N   
309  C  CA  . THR   A 43  ? 0.862 0.322 0.623 0.013  -0.185 -0.053 42  THR   AAA CA  
310  C  C   . THR   A 43  ? 0.809 0.549 0.568 0.001  -0.133 -0.069 42  THR   AAA C   
311  O  O   . THR   A 43  ? 0.574 0.602 0.719 -0.024 -0.203 0.021  42  THR   AAA O   
312  C  CB  . THR   A 43  ? 0.938 0.693 0.466 0.128  -0.190 0.087  42  THR   AAA CB  
313  O  OG1 . THR   A 43  ? 1.306 0.629 0.629 -0.185 -0.079 0.020  42  THR   AAA OG1 
314  C  CG2 . THR   A 43  ? 0.981 0.906 0.490 -0.001 -0.174 0.007  42  THR   AAA CG2 
315  N  N   . SER   A 44  ? 0.711 0.401 0.609 -0.018 -0.181 -0.081 43  SER   AAA N   
316  C  CA  . SER   A 44  ? 0.565 0.470 0.699 0.035  -0.164 -0.012 43  SER   AAA CA  
317  C  C   . SER   A 44  ? 0.490 0.553 0.579 0.140  -0.067 -0.083 43  SER   AAA C   
318  O  O   . SER   A 44  ? 0.522 0.617 0.651 0.088  -0.045 -0.192 43  SER   AAA O   
319  C  CB  . SER   A 44  ? 0.523 0.561 0.726 0.034  -0.184 0.070  43  SER   AAA CB  
320  O  OG  . SER   A 44  ? 0.501 0.253 0.751 0.084  -0.173 -0.063 43  SER   AAA OG  
321  N  N   . LEU   A 45  ? 0.447 0.507 0.455 0.093  -0.048 -0.095 44  LEU   AAA N   
322  C  CA  . LEU   A 45  ? 0.474 0.360 0.460 0.033  -0.053 -0.028 44  LEU   AAA CA  
323  C  C   . LEU   A 45  ? 0.484 0.448 0.407 -0.008 0.022  0.019  44  LEU   AAA C   
324  O  O   . LEU   A 45  ? 0.572 0.333 0.427 -0.089 0.053  0.031  44  LEU   AAA O   
325  C  CB  . LEU   A 45  ? 0.445 0.293 0.514 -0.021 -0.031 -0.025 44  LEU   AAA CB  
326  C  CG  . LEU   A 45  ? 0.399 0.202 0.454 -0.016 -0.056 -0.085 44  LEU   AAA CG  
327  C  CD1 . LEU   A 45  ? 0.438 0.138 0.528 -0.006 -0.029 -0.010 44  LEU   AAA CD1 
328  C  CD2 . LEU   A 45  ? 0.421 0.261 0.477 0.026  -0.022 -0.061 44  LEU   AAA CD2 
329  N  N   . LYS   A 46  ? 0.441 0.384 0.482 0.016  0.009  0.010  45  LYS   AAA N   
330  C  CA  . LYS   A 46  ? 0.427 0.407 0.535 0.033  0.010  0.025  45  LYS   AAA CA  
331  C  C   . LYS   A 46  ? 0.430 0.360 0.477 0.051  0.017  0.016  45  LYS   AAA C   
332  O  O   . LYS   A 46  ? 0.468 0.356 0.484 0.053  -0.023 0.009  45  LYS   AAA O   
333  C  CB  . LYS   A 46  ? 0.398 0.518 0.670 0.138  -0.015 0.098  45  LYS   AAA CB  
334  C  CG  . LYS   A 46  ? 0.371 0.663 0.887 0.012  -0.053 0.115  45  LYS   AAA CG  
335  C  CD  . LYS   A 46  ? 0.475 0.645 1.148 -0.031 -0.039 0.151  45  LYS   AAA CD  
336  C  CE  . LYS   A 46  ? 0.390 0.741 1.260 -0.190 -0.145 0.176  45  LYS   AAA CE  
337  N  NZ  . LYS   A 46  ? 0.607 0.795 1.394 -0.395 -0.136 0.311  45  LYS   AAA NZ  
338  N  N   . PRO   A 47  ? 0.461 0.397 0.446 -0.018 0.005  0.015  46  PRO   AAA N   
339  C  CA  . PRO   A 47  ? 0.503 0.343 0.454 0.017  -0.038 0.018  46  PRO   AAA CA  
340  C  C   . PRO   A 47  ? 0.451 0.216 0.449 0.042  -0.056 0.001  46  PRO   AAA C   
341  O  O   . PRO   A 47  ? 0.491 0.259 0.501 0.043  0.019  0.029  46  PRO   AAA O   
342  C  CB  . PRO   A 47  ? 0.484 0.452 0.470 -0.050 0.010  -0.000 46  PRO   AAA CB  
343  C  CG  . PRO   A 47  ? 0.518 0.349 0.456 0.019  -0.006 -0.057 46  PRO   AAA CG  
344  C  CD  . PRO   A 47  ? 0.549 0.390 0.453 -0.008 -0.026 -0.046 46  PRO   AAA CD  
345  N  N   . ILE   A 48  ? 0.451 0.217 0.471 0.023  -0.067 -0.021 47  ILE   AAA N   
346  C  CA  . ILE   A 48  ? 0.462 0.169 0.450 -0.005 -0.023 0.007  47  ILE   AAA CA  
347  C  C   . ILE   A 48  ? 0.385 0.149 0.412 0.039  0.005  0.034  47  ILE   AAA C   
348  O  O   . ILE   A 48  ? 0.517 0.145 0.522 -0.015 0.071  0.025  47  ILE   AAA O   
349  C  CB  . ILE   A 48  ? 0.615 0.110 0.494 0.022  -0.057 0.027  47  ILE   AAA CB  
350  C  CG1 . ILE   A 48  ? 0.819 0.038 0.501 0.103  0.004  0.015  47  ILE   AAA CG1 
351  C  CG2 . ILE   A 48  ? 0.763 0.145 0.470 0.047  0.011  0.046  47  ILE   AAA CG2 
352  C  CD1 . ILE   A 48  ? 0.788 0.039 0.523 -0.029 -0.007 -0.007 47  ILE   AAA CD1 
353  N  N   . SER   A 49  ? 0.459 0.054 0.473 0.029  0.028  0.016  48  SER   AAA N   
354  C  CA  . SER   A 49  ? 0.586 0.060 0.516 0.069  -0.026 -0.011 48  SER   AAA CA  
355  C  C   . SER   A 49  ? 0.438 0.162 0.502 0.056  -0.023 -0.010 48  SER   AAA C   
356  O  O   . SER   A 49  ? 0.454 0.274 0.431 -0.007 -0.047 -0.024 48  SER   AAA O   
357  C  CB  . SER   A 49  ? 0.649 0.224 0.648 0.141  -0.091 0.018  48  SER   AAA CB  
358  O  OG  . SER   A 49  ? 0.753 0.342 0.584 0.152  -0.058 0.044  48  SER   AAA OG  
359  N  N   . VAL   A 50  ? 0.403 0.122 0.461 0.080  0.017  0.043  49  VAL   AAA N   
360  C  CA  . VAL   A 50  ? 0.489 0.075 0.466 0.028  0.012  0.020  49  VAL   AAA CA  
361  C  C   . VAL   A 50  ? 0.469 0.093 0.469 -0.042 0.012  0.021  49  VAL   AAA C   
362  O  O   . VAL   A 50  ? 0.448 0.201 0.436 0.034  0.031  0.056  49  VAL   AAA O   
363  C  CB  . VAL   A 50  ? 0.519 0.021 0.505 0.082  0.026  -0.022 49  VAL   AAA CB  
364  C  CG1 . VAL   A 50  ? 0.472 0.048 0.496 0.003  -0.008 -0.051 49  VAL   AAA CG1 
365  C  CG2 . VAL   A 50  ? 0.525 0.131 0.578 0.099  0.065  0.058  49  VAL   AAA CG2 
366  N  N   . SER   A 51  ? 0.482 0.018 0.558 -0.027 0.021  0.072  50  SER   AAA N   
367  C  CA  . SER   A 51  ? 0.504 0.012 0.545 -0.030 0.023  0.003  50  SER   AAA CA  
368  C  C   . SER   A 51  ? 0.396 0.050 0.510 0.054  0.028  0.012  50  SER   AAA C   
369  O  O   . SER   A 51  ? 0.405 0.018 0.487 -0.020 0.032  0.041  50  SER   AAA O   
370  C  CB  . SER   A 51  ? 0.584 0.051 0.535 0.057  0.037  0.057  50  SER   AAA CB  
371  O  OG  . SER   A 51  ? 0.714 0.112 0.616 0.007  0.019  0.019  50  SER   AAA OG  
372  N  N   . TYR   A 52  ? 0.402 0.045 0.521 0.071  -0.015 -0.007 51  TYR   AAA N   
373  C  CA  . TYR   A 52  ? 0.436 0.008 0.532 -0.020 0.023  0.014  51  TYR   AAA CA  
374  C  C   . TYR   A 52  ? 0.518 0.013 0.488 -0.036 0.070  -0.049 51  TYR   AAA C   
375  O  O   . TYR   A 52  ? 0.539 0.072 0.586 -0.054 0.131  -0.043 51  TYR   AAA O   
376  C  CB  . TYR   A 52  ? 0.426 0.027 0.519 0.019  -0.030 0.022  51  TYR   AAA CB  
377  C  CG  . TYR   A 52  ? 0.338 0.073 0.469 -0.043 0.014  0.000  51  TYR   AAA CG  
378  C  CD1 . TYR   A 52  ? 0.330 0.010 0.471 -0.009 0.024  -0.039 51  TYR   AAA CD1 
379  C  CD2 . TYR   A 52  ? 0.347 0.009 0.435 -0.021 -0.005 0.023  51  TYR   AAA CD2 
380  C  CE1 . TYR   A 52  ? 0.333 0.008 0.412 -0.017 -0.001 -0.018 51  TYR   AAA CE1 
381  C  CE2 . TYR   A 52  ? 0.401 0.011 0.475 -0.031 -0.001 0.034  51  TYR   AAA CE2 
382  C  CZ  . TYR   A 52  ? 0.342 0.044 0.462 0.006  -0.001 -0.031 51  TYR   AAA CZ  
383  O  OH  . TYR   A 52  ? 0.368 0.016 0.440 0.058  0.016  0.019  51  TYR   AAA OH  
384  N  N   . ASN   A 53  ? 0.431 0.009 0.493 0.032  0.026  0.003  52  ASN   AAA N   
385  C  CA  . ASN   A 53  ? 0.502 0.020 0.505 -0.045 0.044  -0.018 52  ASN   AAA CA  
386  C  C   . ASN   A 53  ? 0.435 0.132 0.422 0.002  0.065  -0.009 52  ASN   AAA C   
387  O  O   . ASN   A 53  ? 0.539 0.011 0.490 0.050  0.032  0.000  52  ASN   AAA O   
388  C  CB  . ASN   A 53  ? 0.491 0.008 0.558 0.013  0.024  0.032  52  ASN   AAA CB  
389  C  CG  . ASN   A 53  ? 0.513 0.010 0.607 0.040  -0.030 0.005  52  ASN   AAA CG  
390  O  OD1 . ASN   A 53  ? 0.507 0.018 0.588 0.076  -0.017 0.008  52  ASN   AAA OD1 
391  N  ND2 . ASN   A 53  ? 0.525 0.030 0.626 0.097  0.017  0.062  52  ASN   AAA ND2 
392  N  N   . PRO   A 54  ? 0.451 0.006 0.442 0.002  0.067  -0.006 53  PRO   AAA N   
393  C  CA  . PRO   A 54  ? 0.398 0.010 0.500 0.020  0.078  -0.015 53  PRO   AAA CA  
394  C  C   . PRO   A 54  ? 0.374 0.035 0.452 -0.040 0.013  -0.007 53  PRO   AAA C   
395  O  O   . PRO   A 54  ? 0.463 0.014 0.459 0.003  -0.019 -0.060 53  PRO   AAA O   
396  C  CB  . PRO   A 54  ? 0.420 0.010 0.530 0.027  0.077  -0.022 53  PRO   AAA CB  
397  C  CG  . PRO   A 54  ? 0.475 0.151 0.573 0.047  0.029  0.073  53  PRO   AAA CG  
398  C  CD  . PRO   A 54  ? 0.482 0.110 0.449 0.011  0.059  0.061  53  PRO   AAA CD  
399  N  N   . ALA   A 55  ? 0.453 0.042 0.513 0.005  0.050  0.070  54  ALA   AAA N   
400  C  CA  . ALA   A 55  ? 0.380 0.080 0.520 -0.000 0.037  0.028  54  ALA   AAA CA  
401  C  C   . ALA   A 55  ? 0.418 0.128 0.432 -0.013 0.057  -0.003 54  ALA   AAA C   
402  O  O   . ALA   A 55  ? 0.518 0.032 0.463 0.075  0.067  -0.031 54  ALA   AAA O   
403  C  CB  . ALA   A 55  ? 0.593 0.116 0.549 0.076  0.052  0.027  54  ALA   AAA CB  
404  N  N   . THR   A 56  ? 0.454 0.041 0.457 0.002  0.060  0.025  55  THR   AAA N   
405  C  CA  . THR   A 56  ? 0.315 0.096 0.454 0.005  0.025  0.035  55  THR   AAA CA  
406  C  C   . THR   A 56  ? 0.339 0.072 0.388 0.045  0.066  -0.018 55  THR   AAA C   
407  O  O   . THR   A 56  ? 0.350 0.022 0.429 0.023  0.011  0.008  55  THR   AAA O   
408  C  CB  . THR   A 56  ? 0.347 0.096 0.406 0.017  -0.001 0.095  55  THR   AAA CB  
409  O  OG1 . THR   A 56  ? 0.388 0.013 0.473 0.051  0.006  -0.013 55  THR   AAA OG1 
410  C  CG2 . THR   A 56  ? 0.375 0.015 0.517 0.057  0.005  0.003  55  THR   AAA CG2 
411  N  N   . ALA   A 57  ? 0.329 0.013 0.444 -0.010 0.006  -0.052 56  ALA   AAA N   
412  C  CA  . ALA   A 57  ? 0.378 0.016 0.454 0.031  0.036  -0.052 56  ALA   AAA CA  
413  C  C   . ALA   A 57  ? 0.394 0.013 0.434 -0.018 0.063  -0.036 56  ALA   AAA C   
414  O  O   . ALA   A 57  ? 0.415 0.036 0.408 0.034  -0.016 -0.071 56  ALA   AAA O   
415  C  CB  . ALA   A 57  ? 0.358 0.012 0.477 0.012  0.013  -0.048 56  ALA   AAA CB  
416  N  N   . LYS   A 58  ? 0.337 0.012 0.433 -0.009 0.048  -0.048 57  LYS   AAA N   
417  C  CA  . LYS   A 58  ? 0.389 0.012 0.457 0.014  0.028  -0.046 57  LYS   AAA CA  
418  C  C   . LYS   A 58  ? 0.375 0.047 0.482 0.073  0.041  -0.086 57  LYS   AAA C   
419  O  O   . LYS   A 58  ? 0.483 0.014 0.540 0.059  0.019  -0.018 57  LYS   AAA O   
420  C  CB  . LYS   A 58  ? 0.357 0.125 0.560 0.084  0.069  0.033  57  LYS   AAA CB  
421  C  CG  . LYS   A 58  ? 0.464 0.114 0.630 0.167  0.125  0.006  57  LYS   AAA CG  
422  C  CD  . LYS   A 58  ? 0.477 0.360 0.831 0.087  0.199  0.119  57  LYS   AAA CD  
423  C  CE  . LYS   A 58  ? 0.581 0.418 0.901 0.006  0.265  0.170  57  LYS   AAA CE  
424  N  NZ  . LYS   A 58  ? 0.614 0.487 1.121 -0.009 0.146  0.255  57  LYS   AAA NZ  
425  N  N   . GLU   A 59  ? 0.355 0.017 0.377 -0.040 0.015  -0.048 58  GLU   AAA N   
426  C  CA  . GLU   A 59  ? 0.360 0.030 0.380 0.009  0.014  -0.084 58  GLU   AAA CA  
427  C  C   . GLU   A 59  ? 0.311 0.046 0.326 0.045  0.010  -0.026 58  GLU   AAA C   
428  O  O   . GLU   A 59  ? 0.361 0.011 0.414 0.037  -0.030 -0.026 58  GLU   AAA O   
429  C  CB  . GLU   A 59  ? 0.455 0.023 0.414 0.082  0.066  -0.010 58  GLU   AAA CB  
430  C  CG  . GLU   A 59  ? 0.424 0.161 0.453 -0.034 0.015  0.010  58  GLU   AAA CG  
431  C  CD  . GLU   A 59  ? 0.411 0.169 0.489 -0.051 0.041  0.027  58  GLU   AAA CD  
432  O  OE1 . GLU   A 59  ? 0.521 0.128 0.545 -0.052 0.075  -0.060 58  GLU   AAA OE1 
433  O  OE2 . GLU   A 59  ? 0.447 0.197 0.578 -0.144 0.058  -0.068 58  GLU   AAA OE2 
434  N  N   . ILE   A 60  ? 0.287 0.016 0.439 0.033  0.015  -0.049 59  ILE   AAA N   
435  C  CA  . ILE   A 60  ? 0.271 0.024 0.367 0.054  0.002  -0.047 59  ILE   AAA CA  
436  C  C   . ILE   A 60  ? 0.306 0.053 0.355 -0.008 -0.013 -0.045 59  ILE   AAA C   
437  O  O   . ILE   A 60  ? 0.321 0.010 0.409 -0.001 -0.019 -0.037 59  ILE   AAA O   
438  C  CB  . ILE   A 60  ? 0.263 0.056 0.372 0.091  0.021  -0.071 59  ILE   AAA CB  
439  C  CG1 . ILE   A 60  ? 0.312 0.012 0.411 0.031  0.011  -0.034 59  ILE   AAA CG1 
440  C  CG2 . ILE   A 60  ? 0.304 0.032 0.417 0.018  0.018  -0.039 59  ILE   AAA CG2 
441  C  CD1 . ILE   A 60  ? 0.324 0.032 0.375 0.078  0.025  -0.042 59  ILE   AAA CD1 
442  N  N   . ILE   A 61  ? 0.305 0.052 0.364 -0.004 0.010  -0.067 60  ILE   AAA N   
443  C  CA  . ILE   A 61  ? 0.335 0.076 0.381 0.057  0.044  -0.039 60  ILE   AAA CA  
444  C  C   . ILE   A 61  ? 0.304 0.044 0.329 0.034  -0.002 -0.024 60  ILE   AAA C   
445  O  O   . ILE   A 61  ? 0.318 0.017 0.392 0.047  -0.003 -0.037 60  ILE   AAA O   
446  C  CB  . ILE   A 61  ? 0.326 0.039 0.415 0.095  0.108  -0.007 60  ILE   AAA CB  
447  C  CG1 . ILE   A 61  ? 0.434 0.027 0.539 0.085  0.053  -0.036 60  ILE   AAA CG1 
448  C  CG2 . ILE   A 61  ? 0.410 0.060 0.419 0.012  0.017  0.020  60  ILE   AAA CG2 
449  C  CD1 . ILE   A 61  ? 0.462 0.374 0.571 -0.050 0.097  -0.066 60  ILE   AAA CD1 
450  N  N   . ASN   A 62  ? 0.326 0.027 0.386 0.069  -0.029 -0.052 61  ASN   AAA N   
451  C  CA  . ASN   A 62  ? 0.305 0.013 0.367 0.045  -0.009 -0.014 61  ASN   AAA CA  
452  C  C   . ASN   A 62  ? 0.275 0.119 0.339 0.029  -0.013 -0.038 61  ASN   AAA C   
453  O  O   . ASN   A 62  ? 0.318 0.038 0.382 0.011  0.016  -0.035 61  ASN   AAA O   
454  C  CB  . ASN   A 62  ? 0.314 0.016 0.396 0.039  0.000  -0.015 61  ASN   AAA CB  
455  C  CG  . ASN   A 62  ? 0.306 0.056 0.424 0.083  -0.014 -0.031 61  ASN   AAA CG  
456  O  OD1 . ASN   A 62  ? 0.351 0.069 0.409 0.045  0.021  -0.002 61  ASN   AAA OD1 
457  N  ND2 . ASN   A 62  ? 0.302 0.090 0.385 0.039  0.005  -0.040 61  ASN   AAA ND2 
458  N  N   . VAL   A 63  ? 0.343 0.022 0.375 -0.011 -0.004 -0.015 62  VAL   AAA N   
459  C  CA  . VAL   A 63  ? 0.354 0.008 0.399 -0.008 -0.004 -0.021 62  VAL   AAA CA  
460  C  C   . VAL   A 63  ? 0.257 0.068 0.411 0.045  -0.015 0.027  62  VAL   AAA C   
461  O  O   . VAL   A 63  ? 0.389 0.092 0.466 -0.049 0.003  -0.028 62  VAL   AAA O   
462  C  CB  . VAL   A 63  ? 0.354 0.008 0.419 -0.027 -0.015 0.003  62  VAL   AAA CB  
463  C  CG1 . VAL   A 63  ? 0.379 0.058 0.472 0.038  0.005  -0.000 62  VAL   AAA CG1 
464  C  CG2 . VAL   A 63  ? 0.337 0.098 0.395 -0.047 -0.055 0.015  62  VAL   AAA CG2 
465  N  N   . GLY   A 64  ? 0.279 0.121 0.429 0.044  -0.012 0.039  63  GLY   AAA N   
466  C  CA  . GLY   A 64  ? 0.358 0.050 0.394 0.008  0.005  0.008  63  GLY   AAA CA  
467  C  C   . GLY   A 64  ? 0.314 0.118 0.354 -0.046 0.005  0.025  63  GLY   AAA C   
468  O  O   . GLY   A 64  ? 0.383 0.155 0.511 0.072  -0.043 -0.092 63  GLY   AAA O   
469  N  N   . HIS   A 65  ? 0.422 0.019 0.388 -0.010 -0.051 0.040  64  HIS   AAA N   
470  C  CA  . HIS   A 65  ? 0.398 0.135 0.400 0.013  -0.018 -0.000 64  HIS   AAA CA  
471  C  C   . HIS   A 65  ? 0.402 0.046 0.382 0.043  0.017  -0.059 64  HIS   AAA C   
472  O  O   . HIS   A 65  ? 0.434 0.049 0.360 0.018  0.048  -0.016 64  HIS   AAA O   
473  C  CB  . HIS   A 65  ? 0.380 0.139 0.376 0.027  -0.033 -0.005 64  HIS   AAA CB  
474  C  CG  . HIS   A 65  ? 0.355 0.030 0.442 -0.005 -0.008 -0.018 64  HIS   AAA CG  
475  N  ND1 . HIS   A 65  ? 0.388 0.125 0.475 -0.029 0.018  -0.003 64  HIS   AAA ND1 
476  C  CD2 . HIS   A 65  ? 0.396 0.016 0.378 -0.046 0.028  -0.043 64  HIS   AAA CD2 
477  C  CE1 . HIS   A 65  ? 0.361 0.029 0.538 -0.030 0.021  -0.024 64  HIS   AAA CE1 
478  N  NE2 . HIS   A 65  ? 0.420 0.014 0.587 -0.057 0.063  -0.018 64  HIS   AAA NE2 
479  N  N   . SER   A 66  ? 0.395 0.040 0.362 0.054  0.024  -0.024 65  SER   AAA N   
480  C  CA  . SER   A 66  ? 0.391 0.046 0.305 -0.014 0.010  -0.053 65  SER   AAA CA  
481  C  C   . SER   A 66  ? 0.329 0.041 0.341 -0.037 -0.033 -0.051 65  SER   AAA C   
482  O  O   . SER   A 66  ? 0.356 0.007 0.372 0.013  0.000  -0.015 65  SER   AAA O   
483  C  CB  . SER   A 66  ? 0.420 0.121 0.315 0.031  -0.008 -0.088 65  SER   AAA CB  
484  O  OG  . SER   A 66  ? 0.443 0.042 0.385 0.051  -0.025 -0.071 65  SER   AAA OG  
485  N  N   . PHE   A 67  ? 0.358 0.035 0.368 0.077  0.011  -0.048 66  PHE   AAA N   
486  C  CA  . PHE   A 67  ? 0.273 0.016 0.369 0.017  -0.013 -0.055 66  PHE   AAA CA  
487  C  C   . PHE   A 67  ? 0.257 0.051 0.341 -0.019 0.006  -0.013 66  PHE   AAA C   
488  O  O   . PHE   A 67  ? 0.329 0.007 0.375 0.012  -0.006 -0.014 66  PHE   AAA O   
489  C  CB  . PHE   A 67  ? 0.273 0.029 0.380 0.032  -0.005 -0.017 66  PHE   AAA CB  
490  C  CG  . PHE   A 67  ? 0.286 0.059 0.355 0.049  0.006  0.010  66  PHE   AAA CG  
491  C  CD1 . PHE   A 67  ? 0.325 0.115 0.378 0.024  0.036  -0.064 66  PHE   AAA CD1 
492  C  CD2 . PHE   A 67  ? 0.322 0.059 0.367 0.030  0.001  0.011  66  PHE   AAA CD2 
493  C  CE1 . PHE   A 67  ? 0.337 0.022 0.407 0.009  0.019  -0.039 66  PHE   AAA CE1 
494  C  CE2 . PHE   A 67  ? 0.335 0.013 0.416 -0.041 0.001  0.027  66  PHE   AAA CE2 
495  C  CZ  . PHE   A 67  ? 0.349 0.061 0.390 -0.029 0.029  -0.002 66  PHE   AAA CZ  
496  N  N   . HIS   A 68  ? 0.270 0.065 0.364 -0.005 -0.001 -0.047 67  HIS   AAA N   
497  C  CA  . HIS   A 68  ? 0.297 0.015 0.395 0.033  -0.016 -0.046 67  HIS   AAA CA  
498  C  C   . HIS   A 68  ? 0.329 0.010 0.381 -0.018 -0.021 -0.032 67  HIS   AAA C   
499  O  O   . HIS   A 68  ? 0.336 0.008 0.384 0.012  -0.021 -0.021 67  HIS   AAA O   
500  C  CB  . HIS   A 68  ? 0.346 0.011 0.436 0.039  0.003  0.010  67  HIS   AAA CB  
501  C  CG  . HIS   A 68  ? 0.373 0.006 0.453 -0.001 -0.003 0.002  67  HIS   AAA CG  
502  N  ND1 . HIS   A 68  ? 0.408 0.008 0.444 0.028  0.016  0.000  67  HIS   AAA ND1 
503  C  CD2 . HIS   A 68  ? 0.283 0.047 0.418 -0.067 0.032  -0.010 67  HIS   AAA CD2 
504  C  CE1 . HIS   A 68  ? 0.409 0.009 0.509 0.023  0.017  -0.026 67  HIS   AAA CE1 
505  N  NE2 . HIS   A 68  ? 0.360 0.009 0.532 0.006  0.043  0.035  67  HIS   AAA NE2 
506  N  N   . VAL   A 69  ? 0.307 0.021 0.372 0.035  -0.006 -0.062 68  VAL   AAA N   
507  C  CA  . VAL   A 69  ? 0.318 0.019 0.397 0.038  -0.009 -0.059 68  VAL   AAA CA  
508  C  C   . VAL   A 69  ? 0.331 0.009 0.355 0.025  0.009  -0.014 68  VAL   AAA C   
509  O  O   . VAL   A 69  ? 0.337 0.015 0.402 0.035  -0.022 -0.046 68  VAL   AAA O   
510  C  CB  . VAL   A 69  ? 0.318 0.014 0.416 0.021  -0.005 -0.053 68  VAL   AAA CB  
511  C  CG1 . VAL   A 69  ? 0.348 0.012 0.423 -0.001 -0.026 -0.050 68  VAL   AAA CG1 
512  C  CG2 . VAL   A 69  ? 0.313 0.102 0.402 -0.024 -0.025 0.055  68  VAL   AAA CG2 
513  N  N   . ASN   A 70  ? 0.291 0.071 0.361 -0.003 0.025  -0.039 69  ASN   AAA N   
514  C  CA  . ASN   A 70  ? 0.296 0.014 0.410 0.023  0.018  -0.045 69  ASN   AAA CA  
515  C  C   . ASN   A 70  ? 0.273 0.014 0.443 0.033  -0.000 -0.040 69  ASN   AAA C   
516  O  O   . ASN   A 70  ? 0.283 0.008 0.437 0.012  -0.002 -0.012 69  ASN   AAA O   
517  C  CB  . ASN   A 70  ? 0.323 0.008 0.453 -0.021 0.037  -0.010 69  ASN   AAA CB  
518  C  CG  . ASN   A 70  ? 0.415 0.025 0.453 -0.069 -0.047 0.062  69  ASN   AAA CG  
519  O  OD1 . ASN   A 70  ? 0.397 0.110 0.506 -0.027 -0.001 -0.022 69  ASN   AAA OD1 
520  N  ND2 . ASN   A 70  ? 0.662 0.296 0.496 -0.157 -0.055 0.175  69  ASN   AAA ND2 
521  N  N   . PHE   A 71  ? 0.307 0.016 0.423 0.048  0.015  0.029  70  PHE   AAA N   
522  C  CA  . PHE   A 71  ? 0.303 0.009 0.442 0.029  0.019  -0.000 70  PHE   AAA CA  
523  C  C   . PHE   A 71  ? 0.343 0.015 0.452 0.047  0.054  -0.021 70  PHE   AAA C   
524  O  O   . PHE   A 71  ? 0.376 0.011 0.509 0.042  0.044  0.010  70  PHE   AAA O   
525  C  CB  . PHE   A 71  ? 0.364 0.009 0.433 0.002  0.031  -0.032 70  PHE   AAA CB  
526  C  CG  . PHE   A 71  ? 0.370 0.009 0.425 -0.001 0.055  -0.035 70  PHE   AAA CG  
527  C  CD1 . PHE   A 71  ? 0.378 0.016 0.408 0.040  0.017  -0.044 70  PHE   AAA CD1 
528  C  CD2 . PHE   A 71  ? 0.340 0.008 0.395 0.008  0.048  -0.019 70  PHE   AAA CD2 
529  C  CE1 . PHE   A 71  ? 0.381 0.084 0.377 0.010  0.012  -0.033 70  PHE   AAA CE1 
530  C  CE2 . PHE   A 71  ? 0.345 0.017 0.433 0.035  0.034  -0.050 70  PHE   AAA CE2 
531  C  CZ  . PHE   A 71  ? 0.360 0.028 0.492 0.057  0.038  -0.072 70  PHE   AAA CZ  
532  N  N   . GLU   A 72  ? 0.334 0.010 0.458 -0.013 0.021  -0.041 71  GLU   AAA N   
533  C  CA  . GLU   A 72  ? 0.326 0.007 0.501 -0.006 0.005  0.016  71  GLU   AAA CA  
534  C  C   . GLU   A 72  ? 0.324 0.025 0.452 0.044  0.040  -0.046 71  GLU   AAA C   
535  O  O   . GLU   A 72  ? 0.386 0.011 0.471 0.034  0.010  -0.002 71  GLU   AAA O   
536  C  CB  . GLU   A 72  ? 0.368 0.010 0.564 0.037  0.001  -0.011 71  GLU   AAA CB  
537  C  CG  . GLU   A 72  ? 0.451 0.145 0.585 0.089  -0.045 -0.050 71  GLU   AAA CG  
538  C  CD  . GLU   A 72  ? 0.530 0.146 0.639 0.014  -0.033 -0.038 71  GLU   AAA CD  
539  O  OE1 . GLU   A 72  ? 0.610 0.058 0.677 0.065  -0.038 -0.042 71  GLU   AAA OE1 
540  O  OE2 . GLU   A 72  ? 0.518 0.112 0.688 0.047  -0.019 -0.105 71  GLU   AAA OE2 
541  N  N   . ASP   A 73  ? 0.348 0.045 0.477 0.025  0.043  -0.044 72  ASP   AAA N   
542  C  CA  . ASP   A 73  ? 0.375 0.017 0.527 0.058  -0.003 -0.030 72  ASP   AAA CA  
543  C  C   . ASP   A 73  ? 0.363 0.143 0.562 0.077  -0.009 -0.126 72  ASP   AAA C   
544  O  O   . ASP   A 73  ? 0.333 0.189 0.532 0.058  0.032  -0.061 72  ASP   AAA O   
545  C  CB  . ASP   A 73  ? 0.388 0.017 0.543 0.044  0.014  -0.054 72  ASP   AAA CB  
546  C  CG  . ASP   A 73  ? 0.473 0.114 0.493 -0.053 0.024  -0.093 72  ASP   AAA CG  
547  O  OD1 . ASP   A 73  ? 0.431 0.207 0.436 -0.037 0.060  -0.053 72  ASP   AAA OD1 
548  O  OD2 . ASP   A 73  ? 0.417 0.075 0.499 0.021  -0.037 -0.120 72  ASP   AAA OD2 
549  N  N   . ASN   A 74  ? 0.345 0.065 0.537 0.024  0.027  -0.034 73  ASN   AAA N   
550  C  CA  . ASN   A 74  ? 0.334 0.161 0.612 0.059  -0.014 -0.055 73  ASN   AAA CA  
551  C  C   . ASN   A 74  ? 0.365 0.108 0.572 0.038  -0.003 -0.094 73  ASN   AAA C   
552  O  O   . ASN   A 74  ? 0.448 0.279 0.663 0.159  0.054  0.050  73  ASN   AAA O   
553  C  CB  . ASN   A 74  ? 0.436 0.174 0.561 0.128  0.015  -0.051 73  ASN   AAA CB  
554  C  CG  . ASN   A 74  ? 0.512 0.201 0.688 0.054  -0.054 0.011  73  ASN   AAA CG  
555  O  OD1 . ASN   A 74  ? 0.710 0.210 0.870 0.215  -0.003 -0.077 73  ASN   AAA OD1 
556  N  ND2 . ASN   A 74  ? 0.478 0.059 0.595 0.025  0.001  -0.088 73  ASN   AAA ND2 
557  N  N   . ASP   A 75  ? 0.412 0.176 0.574 0.086  0.011  -0.093 74  ASP   AAA N   
558  C  CA  . ASP   A 75  ? 0.558 0.099 0.627 0.059  0.030  -0.063 74  ASP   AAA CA  
559  C  C   . ASP   A 75  ? 0.431 0.142 0.588 0.054  -0.013 -0.032 74  ASP   AAA C   
560  O  O   . ASP   A 75  ? 0.410 0.111 0.597 0.053  0.066  -0.032 74  ASP   AAA O   
561  C  CB  . ASP   A 75  ? 0.565 0.084 0.616 0.064  0.047  -0.004 74  ASP   AAA CB  
562  C  CG  . ASP   A 75  ? 0.655 0.067 0.691 0.019  0.025  -0.117 74  ASP   AAA CG  
563  O  OD1 . ASP   A 75  ? 0.549 0.146 0.618 -0.016 0.095  -0.013 74  ASP   AAA OD1 
564  O  OD2 . ASP   A 75  ? 0.598 0.057 0.827 0.049  0.048  -0.112 74  ASP   AAA OD2 
565  N  N   . ASN   A 76  ? 0.408 0.141 0.594 0.081  0.019  0.002  75  ASN   AAA N   
566  C  CA  . ASN   A 76  ? 0.426 0.063 0.651 0.151  0.029  -0.032 75  ASN   AAA CA  
567  C  C   . ASN   A 76  ? 0.476 0.033 0.483 0.110  -0.023 0.015  75  ASN   AAA C   
568  O  O   . ASN   A 76  ? 0.543 0.150 0.493 0.138  0.001  0.004  75  ASN   AAA O   
569  C  CB  . ASN   A 76  ? 0.500 0.095 0.677 0.185  -0.009 -0.008 75  ASN   AAA CB  
570  C  CG  . ASN   A 76  ? 0.486 0.245 0.631 0.081  -0.029 0.185  75  ASN   AAA CG  
571  O  OD1 . ASN   A 76  ? 0.489 0.060 0.655 0.055  -0.077 0.017  75  ASN   AAA OD1 
572  N  ND2 . ASN   A 76  ? 0.581 0.451 0.767 -0.081 -0.215 0.065  75  ASN   AAA ND2 
573  N  N   . ARG   A 77  ? 0.361 0.147 0.538 0.118  0.003  0.004  76  ARG   AAA N   
574  C  CA  . ARG   A 77  ? 0.397 0.050 0.516 0.123  -0.008 0.049  76  ARG   AAA CA  
575  C  C   . ARG   A 77  ? 0.452 0.018 0.574 0.003  0.055  -0.079 76  ARG   AAA C   
576  O  O   . ARG   A 77  ? 0.505 0.101 0.525 0.046  0.020  -0.025 76  ARG   AAA O   
577  C  CB  . ARG   A 77  ? 0.429 0.029 0.569 0.094  0.008  -0.034 76  ARG   AAA CB  
578  C  CG  . ARG   A 77  ? 0.520 0.055 0.586 0.152  -0.010 -0.049 76  ARG   AAA CG  
579  C  CD  . ARG   A 77  ? 0.522 0.019 0.560 -0.012 0.015  -0.016 76  ARG   AAA CD  
580  N  NE  . ARG   A 77  ? 0.420 0.010 0.531 0.031  -0.046 -0.026 76  ARG   AAA NE  
581  C  CZ  . ARG   A 77  ? 0.446 0.153 0.494 0.072  -0.025 -0.008 76  ARG   AAA CZ  
582  N  NH1 . ARG   A 77  ? 0.444 0.065 0.548 0.108  -0.018 -0.009 76  ARG   AAA NH1 
583  N  NH2 . ARG   A 77  ? 0.487 0.107 0.513 0.045  0.047  -0.045 76  ARG   AAA NH2 
584  N  N   . SER   A 78  ? 0.452 0.008 0.474 -0.017 0.031  -0.027 77  SER   AAA N   
585  C  CA  . SER   A 78  ? 0.361 0.115 0.372 -0.026 0.013  -0.031 77  SER   AAA CA  
586  C  C   . SER   A 78  ? 0.347 0.080 0.410 0.016  -0.008 -0.029 77  SER   AAA C   
587  O  O   . SER   A 78  ? 0.385 0.095 0.469 0.080  0.048  0.012  77  SER   AAA O   
588  C  CB  . SER   A 78  ? 0.354 0.041 0.376 0.063  0.025  -0.031 77  SER   AAA CB  
589  O  OG  . SER   A 78  ? 0.430 0.036 0.447 0.079  -0.021 -0.046 77  SER   AAA OG  
590  N  N   . VAL   A 79  ? 0.401 0.033 0.420 0.048  -0.016 0.005  78  VAL   AAA N   
591  C  CA  . VAL   A 79  ? 0.361 0.055 0.464 -0.031 0.003  0.025  78  VAL   AAA CA  
592  C  C   . VAL   A 79  ? 0.328 0.162 0.469 0.030  0.019  0.032  78  VAL   AAA C   
593  O  O   . VAL   A 79  ? 0.406 0.051 0.479 0.002  0.029  -0.041 78  VAL   AAA O   
594  C  CB  . VAL   A 79  ? 0.393 0.073 0.534 0.028  0.025  0.030  78  VAL   AAA CB  
595  C  CG1 . VAL   A 79  ? 0.399 0.132 0.532 0.003  -0.007 -0.009 78  VAL   AAA CG1 
596  C  CG2 . VAL   A 79  ? 0.533 0.022 0.616 0.091  -0.004 -0.012 78  VAL   AAA CG2 
597  N  N   . LEU   A 80  ? 0.409 0.153 0.428 0.055  0.007  -0.010 79  LEU   AAA N   
598  C  CA  . LEU   A 80  ? 0.394 0.120 0.392 0.037  0.008  0.014  79  LEU   AAA CA  
599  C  C   . LEU   A 80  ? 0.408 0.063 0.438 0.097  -0.003 -0.014 79  LEU   AAA C   
600  O  O   . LEU   A 80  ? 0.369 0.125 0.502 0.070  -0.025 -0.005 79  LEU   AAA O   
601  C  CB  . LEU   A 80  ? 0.380 0.094 0.380 0.005  0.002  0.005  79  LEU   AAA CB  
602  C  CG  . LEU   A 80  ? 0.430 0.200 0.397 0.106  -0.037 -0.060 79  LEU   AAA CG  
603  C  CD1 . LEU   A 80  ? 0.493 0.207 0.404 0.109  -0.041 -0.105 79  LEU   AAA CD1 
604  C  CD2 . LEU   A 80  ? 0.454 0.192 0.399 0.058  -0.010 -0.024 79  LEU   AAA CD2 
605  N  N   . LYS   A 81  ? 0.473 0.052 0.464 0.067  -0.023 0.030  80  LYS   AAA N   
606  C  CA  . LYS   A 81  ? 0.539 0.235 0.476 0.070  -0.073 0.006  80  LYS   AAA CA  
607  C  C   . LYS   A 81  ? 0.393 0.125 0.458 0.102  -0.085 0.054  80  LYS   AAA C   
608  O  O   . LYS   A 81  ? 0.374 0.282 0.450 0.026  -0.033 -0.003 80  LYS   AAA O   
609  C  CB  . LYS   A 81  ? 0.584 0.256 0.632 0.076  -0.185 0.009  80  LYS   AAA CB  
610  C  CG  . LYS   A 81  ? 0.872 0.132 0.921 0.039  -0.080 -0.110 80  LYS   AAA CG  
611  C  CD  . LYS   A 81  ? 1.040 0.323 1.138 0.317  -0.235 0.013  80  LYS   AAA CD  
612  C  CE  . LYS   A 81  ? 0.973 0.514 1.354 0.260  -0.226 0.011  80  LYS   AAA CE  
613  N  NZ  . LYS   A 81  ? 1.012 0.539 1.611 0.066  -0.379 0.250  80  LYS   AAA NZ  
614  N  N   . GLY   A 82  ? 0.390 0.249 0.484 0.112  -0.073 0.004  81  GLY   AAA N   
615  C  CA  . GLY   A 82  ? 0.451 0.155 0.471 0.048  -0.080 -0.011 81  GLY   AAA CA  
616  C  C   . GLY   A 82  ? 0.382 0.154 0.433 0.040  -0.010 0.038  81  GLY   AAA C   
617  O  O   . GLY   A 82  ? 0.456 0.083 0.440 0.005  -0.015 -0.011 81  GLY   AAA O   
618  N  N   . GLY   A 83  ? 0.399 0.112 0.499 0.042  0.009  0.045  82  GLY   AAA N   
619  C  CA  . GLY   A 83  ? 0.496 0.136 0.454 0.070  -0.046 -0.012 82  GLY   AAA CA  
620  C  C   . GLY   A 83  ? 0.509 0.192 0.454 -0.001 -0.042 -0.005 82  GLY   AAA C   
621  O  O   . GLY   A 83  ? 0.437 0.322 0.497 -0.002 -0.066 -0.043 82  GLY   AAA O   
622  N  N   . PRO   A 84  ? 0.374 0.230 0.437 0.054  -0.029 0.016  83  PRO   AAA N   
623  C  CA  . PRO   A 84  ? 0.390 0.301 0.455 0.012  -0.028 0.013  83  PRO   AAA CA  
624  C  C   . PRO   A 84  ? 0.359 0.309 0.503 -0.022 -0.052 -0.056 83  PRO   AAA C   
625  O  O   . PRO   A 84  ? 0.356 0.309 0.658 -0.013 -0.040 -0.011 83  PRO   AAA O   
626  C  CB  . PRO   A 84  ? 0.469 0.219 0.462 -0.030 0.010  -0.026 83  PRO   AAA CB  
627  C  CG  . PRO   A 84  ? 0.438 0.273 0.471 -0.036 0.031  -0.079 83  PRO   AAA CG  
628  C  CD  . PRO   A 84  ? 0.395 0.308 0.409 -0.007 -0.044 0.018  83  PRO   AAA CD  
629  N  N   . PHE   A 85  ? 0.395 0.244 0.474 0.072  -0.049 -0.043 84  PHE   AAA N   
630  C  CA  . PHE   A 85  ? 0.392 0.414 0.414 0.062  -0.059 -0.010 84  PHE   AAA CA  
631  C  C   . PHE   A 85  ? 0.403 0.366 0.443 0.024  -0.067 0.030  84  PHE   AAA C   
632  O  O   . PHE   A 85  ? 0.428 0.315 0.517 0.090  -0.058 0.102  84  PHE   AAA O   
633  C  CB  . PHE   A 85  ? 0.384 0.307 0.440 0.075  -0.052 -0.014 84  PHE   AAA CB  
634  C  CG  . PHE   A 85  ? 0.368 0.403 0.433 0.083  -0.053 0.030  84  PHE   AAA CG  
635  C  CD1 . PHE   A 85  ? 0.384 0.214 0.519 0.125  -0.032 -0.068 84  PHE   AAA CD1 
636  C  CD2 . PHE   A 85  ? 0.383 0.382 0.439 0.048  -0.049 0.029  84  PHE   AAA CD2 
637  C  CE1 . PHE   A 85  ? 0.389 0.257 0.529 0.113  -0.022 -0.028 84  PHE   AAA CE1 
638  C  CE2 . PHE   A 85  ? 0.379 0.192 0.504 0.072  -0.021 -0.069 84  PHE   AAA CE2 
639  C  CZ  . PHE   A 85  ? 0.393 0.320 0.422 0.055  -0.034 0.034  84  PHE   AAA CZ  
640  N  N   . SER   A 86  ? 0.412 0.406 0.549 0.088  -0.036 -0.035 85  SER   AAA N   
641  C  CA  . SER   A 86  ? 0.424 0.269 0.618 0.043  -0.025 -0.037 85  SER   AAA CA  
642  C  C   . SER   A 86  ? 0.456 0.159 0.607 0.044  -0.089 0.002  85  SER   AAA C   
643  O  O   . SER   A 86  ? 0.558 0.245 0.853 0.221  0.040  0.148  85  SER   AAA O   
644  C  CB  . SER   A 86  ? 0.445 0.354 0.911 -0.004 -0.078 -0.027 85  SER   AAA CB  
645  O  OG  . SER   A 86  ? 0.621 0.547 1.044 0.015  -0.134 -0.109 85  SER   AAA OG  
646  N  N   . ASP   A 87  ? 0.401 0.355 0.535 0.051  -0.045 -0.013 86  ASP   AAA N   
647  C  CA  . ASP   A 87  ? 0.395 0.550 0.546 0.047  -0.006 -0.059 86  ASP   AAA CA  
648  C  C   . ASP   A 87  ? 0.405 0.280 0.515 0.069  0.015  -0.063 86  ASP   AAA C   
649  O  O   . ASP   A 87  ? 0.361 0.331 0.611 0.067  0.006  -0.111 86  ASP   AAA O   
650  C  CB  . ASP   A 87  ? 0.406 0.537 0.601 0.125  0.040  -0.039 86  ASP   AAA CB  
651  C  CG  . ASP   A 87  ? 0.448 0.448 0.560 0.105  -0.036 0.051  86  ASP   AAA CG  
652  O  OD1 . ASP   A 87  ? 0.439 0.534 0.655 0.197  -0.074 -0.024 86  ASP   AAA OD1 
653  O  OD2 . ASP   A 87  ? 0.438 0.483 0.487 -0.028 -0.031 0.022  86  ASP   AAA OD2 
654  N  N   . SER   A 88  ? 0.396 0.386 0.504 0.096  -0.067 -0.091 87  SER   AAA N   
655  C  CA  . SER   A 88  ? 0.389 0.214 0.599 0.072  -0.047 -0.012 87  SER   AAA CA  
656  C  C   . SER   A 88  ? 0.292 0.221 0.528 0.042  0.034  -0.028 87  SER   AAA C   
657  O  O   . SER   A 88  ? 0.336 0.197 0.544 -0.010 0.047  -0.030 87  SER   AAA O   
658  C  CB  . SER   A 88  ? 0.461 0.194 0.689 0.040  -0.089 0.011  87  SER   AAA CB  
659  O  OG  . SER   A 88  ? 0.528 0.440 0.747 -0.115 -0.057 0.066  87  SER   AAA OG  
660  N  N   . TYR   A 89  ? 0.339 0.096 0.503 0.056  -0.043 -0.022 88  TYR   AAA N   
661  C  CA  . TYR   A 89  ? 0.299 0.119 0.463 0.067  -0.016 -0.047 88  TYR   AAA CA  
662  C  C   . TYR   A 89  ? 0.301 0.103 0.397 0.051  0.011  -0.018 88  TYR   AAA C   
663  O  O   . TYR   A 89  ? 0.376 0.100 0.496 -0.011 0.009  0.041  88  TYR   AAA O   
664  C  CB  . TYR   A 89  ? 0.302 0.012 0.441 0.027  -0.014 0.034  88  TYR   AAA CB  
665  C  CG  . TYR   A 89  ? 0.266 0.191 0.431 -0.037 -0.013 0.001  88  TYR   AAA CG  
666  C  CD1 . TYR   A 89  ? 0.292 0.142 0.455 0.031  -0.045 -0.073 88  TYR   AAA CD1 
667  C  CD2 . TYR   A 89  ? 0.326 0.047 0.436 0.055  -0.035 -0.046 88  TYR   AAA CD2 
668  C  CE1 . TYR   A 89  ? 0.272 0.203 0.457 -0.010 -0.015 -0.037 88  TYR   AAA CE1 
669  C  CE2 . TYR   A 89  ? 0.294 0.141 0.462 -0.004 0.013  -0.079 88  TYR   AAA CE2 
670  C  CZ  . TYR   A 89  ? 0.357 0.114 0.416 -0.008 0.008  -0.109 88  TYR   AAA CZ  
671  O  OH  . TYR   A 89  ? 0.367 0.189 0.542 -0.009 -0.009 -0.166 88  TYR   AAA OH  
672  N  N   . ARG   A 90  ? 0.302 0.131 0.402 0.085  -0.022 -0.030 89  ARG   AAA N   
673  C  CA  . ARG   A 90  ? 0.286 0.114 0.394 0.007  -0.017 0.025  89  ARG   AAA CA  
674  C  C   . ARG   A 90  ? 0.262 0.162 0.347 -0.001 0.010  0.043  89  ARG   AAA C   
675  O  O   . ARG   A 90  ? 0.334 0.074 0.375 0.055  -0.010 0.009  89  ARG   AAA O   
676  C  CB  . ARG   A 90  ? 0.333 0.105 0.403 0.028  -0.007 0.026  89  ARG   AAA CB  
677  C  CG  . ARG   A 90  ? 0.344 0.165 0.471 0.024  -0.004 -0.031 89  ARG   AAA CG  
678  C  CD  . ARG   A 90  ? 0.413 0.269 0.473 0.022  0.039  -0.051 89  ARG   AAA CD  
679  N  NE  . ARG   A 90  ? 0.410 0.148 0.519 -0.041 -0.014 -0.036 89  ARG   AAA NE  
680  C  CZ  . ARG   A 90  ? 0.404 0.101 0.555 0.003  -0.027 -0.002 89  ARG   AAA CZ  
681  N  NH1 . ARG   A 90  ? 0.336 0.171 0.534 0.093  -0.029 -0.046 89  ARG   AAA NH1 
682  N  NH2 . ARG   A 90  ? 0.450 0.229 0.631 0.013  -0.098 -0.010 89  ARG   AAA NH2 
683  N  N   . LEU   A 91  ? 0.288 0.121 0.388 -0.028 0.003  -0.037 90  LEU   AAA N   
684  C  CA  . LEU   A 91  ? 0.297 0.040 0.404 0.025  0.008  -0.032 90  LEU   AAA CA  
685  C  C   . LEU   A 91  ? 0.284 0.052 0.402 0.085  0.016  0.026  90  LEU   AAA C   
686  O  O   . LEU   A 91  ? 0.370 0.083 0.367 0.036  0.035  -0.023 90  LEU   AAA O   
687  C  CB  . LEU   A 91  ? 0.280 0.019 0.453 0.046  0.024  -0.045 90  LEU   AAA CB  
688  C  CG  . LEU   A 91  ? 0.301 0.013 0.407 0.042  0.030  -0.013 90  LEU   AAA CG  
689  C  CD1 . LEU   A 91  ? 0.351 0.007 0.470 -0.004 -0.015 0.010  90  LEU   AAA CD1 
690  C  CD2 . LEU   A 91  ? 0.295 0.110 0.441 -0.029 0.046  -0.025 90  LEU   AAA CD2 
691  N  N   . PHE   A 92  ? 0.271 0.016 0.402 0.035  -0.003 -0.046 91  PHE   AAA N   
692  C  CA  . PHE   A 92  ? 0.288 0.009 0.416 0.009  0.022  -0.033 91  PHE   AAA CA  
693  C  C   . PHE   A 92  ? 0.301 0.008 0.347 0.020  0.035  0.009  91  PHE   AAA C   
694  O  O   . PHE   A 92  ? 0.341 0.008 0.387 0.021  -0.003 -0.002 91  PHE   AAA O   
695  C  CB  . PHE   A 92  ? 0.275 0.054 0.413 -0.002 0.015  -0.038 91  PHE   AAA CB  
696  C  CG  . PHE   A 92  ? 0.273 0.051 0.374 0.022  -0.024 -0.030 91  PHE   AAA CG  
697  C  CD1 . PHE   A 92  ? 0.297 0.008 0.371 0.016  -0.015 -0.016 91  PHE   AAA CD1 
698  C  CD2 . PHE   A 92  ? 0.312 0.015 0.384 -0.011 -0.027 -0.043 91  PHE   AAA CD2 
699  C  CE1 . PHE   A 92  ? 0.293 0.026 0.394 0.011  -0.023 -0.088 91  PHE   AAA CE1 
700  C  CE2 . PHE   A 92  ? 0.315 0.007 0.397 0.013  0.002  -0.008 91  PHE   AAA CE2 
701  C  CZ  . PHE   A 92  ? 0.293 0.151 0.370 0.037  0.002  -0.033 91  PHE   AAA CZ  
702  N  N   . GLN   A 93  ? 0.271 0.031 0.425 0.002  0.027  -0.074 92  GLN   AAA N   
703  C  CA  . GLN   A 93  ? 0.255 0.030 0.423 -0.044 0.022  -0.031 92  GLN   AAA CA  
704  C  C   . GLN   A 93  ? 0.238 0.063 0.344 -0.002 -0.014 0.017  92  GLN   AAA C   
705  O  O   . GLN   A 93  ? 0.271 0.059 0.356 0.052  -0.016 -0.028 92  GLN   AAA O   
706  C  CB  . GLN   A 93  ? 0.276 0.052 0.444 -0.005 0.056  -0.002 92  GLN   AAA CB  
707  C  CG  . GLN   A 93  ? 0.329 0.173 0.437 -0.019 0.010  -0.005 92  GLN   AAA CG  
708  C  CD  . GLN   A 93  ? 0.347 0.093 0.453 0.018  0.076  -0.086 92  GLN   AAA CD  
709  O  OE1 . GLN   A 93  ? 0.491 0.182 0.488 0.083  0.124  -0.037 92  GLN   AAA OE1 
710  N  NE2 . GLN   A 93  ? 0.293 0.067 0.448 0.038  0.016  -0.069 92  GLN   AAA NE2 
711  N  N   . PHE   A 94  ? 0.242 0.021 0.366 -0.002 -0.016 -0.067 93  PHE   AAA N   
712  C  CA  . PHE   A 94  ? 0.246 0.018 0.384 0.015  -0.011 -0.064 93  PHE   AAA CA  
713  C  C   . PHE   A 94  ? 0.285 0.029 0.313 0.028  -0.020 -0.080 93  PHE   AAA C   
714  O  O   . PHE   A 94  ? 0.294 0.039 0.333 0.023  -0.002 -0.050 93  PHE   AAA O   
715  C  CB  . PHE   A 94  ? 0.272 0.112 0.360 0.022  -0.002 -0.044 93  PHE   AAA CB  
716  C  CG  . PHE   A 94  ? 0.293 0.010 0.366 0.029  -0.017 -0.015 93  PHE   AAA CG  
717  C  CD1 . PHE   A 94  ? 0.234 0.131 0.410 -0.019 -0.013 -0.022 93  PHE   AAA CD1 
718  C  CD2 . PHE   A 94  ? 0.274 0.016 0.372 0.029  -0.039 -0.055 93  PHE   AAA CD2 
719  C  CE1 . PHE   A 94  ? 0.251 0.021 0.397 0.037  -0.009 -0.060 93  PHE   AAA CE1 
720  C  CE2 . PHE   A 94  ? 0.294 0.017 0.416 -0.025 -0.020 -0.024 93  PHE   AAA CE2 
721  C  CZ  . PHE   A 94  ? 0.277 0.016 0.432 -0.035 -0.000 -0.047 93  PHE   AAA CZ  
722  N  N   . HIS   A 95  ? 0.315 0.022 0.364 -0.004 -0.026 -0.074 94  HIS   AAA N   
723  C  CA  . HIS   A 95  ? 0.277 0.076 0.326 -0.004 -0.014 -0.055 94  HIS   AAA CA  
724  C  C   . HIS   A 95  ? 0.255 0.009 0.375 -0.018 -0.004 -0.022 94  HIS   AAA C   
725  O  O   . HIS   A 95  ? 0.359 0.010 0.403 0.032  0.007  -0.017 94  HIS   AAA O   
726  C  CB  . HIS   A 95  ? 0.235 0.044 0.364 0.035  0.011  -0.065 94  HIS   AAA CB  
727  C  CG  . HIS   A 95  ? 0.278 0.039 0.382 0.029  -0.012 -0.062 94  HIS   AAA CG  
728  N  ND1 . HIS   A 95  ? 0.275 0.011 0.481 0.019  -0.021 -0.041 94  HIS   AAA ND1 
729  C  CD2 . HIS   A 95  ? 0.257 0.027 0.383 0.066  0.005  -0.031 94  HIS   AAA CD2 
730  C  CE1 . HIS   A 95  ? 0.261 0.086 0.437 -0.027 0.014  -0.112 94  HIS   AAA CE1 
731  N  NE2 . HIS   A 95  ? 0.345 0.007 0.492 -0.016 0.000  -0.009 94  HIS   AAA NE2 
732  N  N   . PHE   A 96  ? 0.295 0.015 0.325 0.018  -0.023 -0.043 95  PHE   AAA N   
733  C  CA  . PHE   A 96  ? 0.273 0.009 0.357 -0.009 -0.006 -0.029 95  PHE   AAA CA  
734  C  C   . PHE   A 96  ? 0.307 0.009 0.357 -0.026 0.009  -0.017 95  PHE   AAA C   
735  O  O   . PHE   A 96  ? 0.290 0.007 0.393 0.015  0.020  -0.006 95  PHE   AAA O   
736  C  CB  . PHE   A 96  ? 0.265 0.101 0.365 0.013  -0.000 0.011  95  PHE   AAA CB  
737  C  CG  . PHE   A 96  ? 0.274 0.080 0.347 0.015  0.018  -0.033 95  PHE   AAA CG  
738  C  CD1 . PHE   A 96  ? 0.334 0.007 0.347 0.007  0.007  0.005  95  PHE   AAA CD1 
739  C  CD2 . PHE   A 96  ? 0.302 0.011 0.365 -0.009 -0.004 -0.034 95  PHE   AAA CD2 
740  C  CE1 . PHE   A 96  ? 0.270 0.015 0.396 -0.007 0.008  -0.056 95  PHE   AAA CE1 
741  C  CE2 . PHE   A 96  ? 0.297 0.008 0.355 -0.017 0.013  -0.012 95  PHE   AAA CE2 
742  C  CZ  . PHE   A 96  ? 0.312 0.014 0.402 0.015  0.001  -0.051 95  PHE   AAA CZ  
743  N  N   . HIS   A 97  ? 0.274 0.074 0.351 0.056  -0.013 -0.032 96  HIS   AAA N   
744  C  CA  . HIS   A 97  ? 0.266 0.045 0.363 0.011  -0.026 -0.036 96  HIS   AAA CA  
745  C  C   . HIS   A 97  ? 0.279 0.085 0.310 -0.003 -0.008 -0.014 96  HIS   AAA C   
746  O  O   . HIS   A 97  ? 0.304 0.030 0.336 0.035  0.015  -0.030 96  HIS   AAA O   
747  C  CB  . HIS   A 97  ? 0.278 0.018 0.388 0.031  -0.000 -0.055 96  HIS   AAA CB  
748  C  CG  . HIS   A 97  ? 0.265 0.018 0.348 0.034  0.030  -0.040 96  HIS   AAA CG  
749  N  ND1 . HIS   A 97  ? 0.278 0.008 0.372 -0.000 0.028  -0.028 96  HIS   AAA ND1 
750  C  CD2 . HIS   A 97  ? 0.271 0.064 0.392 0.086  0.026  -0.051 96  HIS   AAA CD2 
751  C  CE1 . HIS   A 97  ? 0.238 0.065 0.341 -0.040 -0.015 0.010  96  HIS   AAA CE1 
752  N  NE2 . HIS   A 97  ? 0.321 0.046 0.368 0.108  0.042  -0.016 96  HIS   AAA NE2 
753  N  N   . TRP   A 98  ? 0.304 0.007 0.403 -0.010 0.022  -0.013 97  TRP   AAA N   
754  C  CA  . TRP   A 98  ? 0.299 0.008 0.438 0.012  -0.000 -0.018 97  TRP   AAA CA  
755  C  C   . TRP   A 98  ? 0.334 0.014 0.414 0.046  0.042  -0.012 97  TRP   AAA C   
756  O  O   . TRP   A 98  ? 0.380 0.010 0.410 0.003  0.035  -0.036 97  TRP   AAA O   
757  C  CB  . TRP   A 98  ? 0.271 0.006 0.403 -0.005 -0.014 -0.001 97  TRP   AAA CB  
758  C  CG  . TRP   A 98  ? 0.300 0.008 0.394 -0.025 -0.007 -0.002 97  TRP   AAA CG  
759  C  CD1 . TRP   A 98  ? 0.372 0.009 0.411 0.026  -0.018 -0.013 97  TRP   AAA CD1 
760  C  CD2 . TRP   A 98  ? 0.278 0.093 0.359 0.024  -0.027 -0.033 97  TRP   AAA CD2 
761  N  NE1 . TRP   A 98  ? 0.352 0.009 0.374 0.028  -0.031 0.016  97  TRP   AAA NE1 
762  C  CE2 . TRP   A 98  ? 0.277 0.032 0.370 0.047  -0.025 0.003  97  TRP   AAA CE2 
763  C  CE3 . TRP   A 98  ? 0.282 0.032 0.419 0.005  -0.009 -0.034 97  TRP   AAA CE3 
764  C  CZ2 . TRP   A 98  ? 0.275 0.067 0.375 0.055  -0.007 0.003  97  TRP   AAA CZ2 
765  C  CZ3 . TRP   A 98  ? 0.279 0.007 0.362 -0.001 -0.035 0.010  97  TRP   AAA CZ3 
766  C  CH2 . TRP   A 98  ? 0.255 0.076 0.336 0.055  -0.023 -0.047 97  TRP   AAA CH2 
767  N  N   . GLY   A 99  ? 0.328 0.021 0.440 0.054  -0.006 -0.050 98  GLY   AAA N   
768  C  CA  . GLY   A 99  ? 0.383 0.019 0.452 0.058  0.044  -0.034 98  GLY   AAA CA  
769  C  C   . GLY   A 99  ? 0.391 0.196 0.480 0.072  0.013  -0.006 98  GLY   AAA C   
770  O  O   . GLY   A 99  ? 0.350 0.191 0.468 0.108  -0.005 0.050  98  GLY   AAA O   
771  N  N   . SER   A 100 ? 0.440 0.287 0.508 0.146  -0.007 0.034  99  SER   AAA N   
772  C  CA  . SER   A 100 ? 0.486 0.470 0.542 0.145  -0.046 0.066  99  SER   AAA CA  
773  C  C   . SER   A 100 ? 0.621 0.457 0.512 0.214  0.076  0.067  99  SER   AAA C   
774  O  O   . SER   A 100 ? 0.571 0.333 0.644 0.197  0.074  0.099  99  SER   AAA O   
775  C  CB  . SER   A 100 ? 0.680 0.366 0.583 0.265  -0.074 0.023  99  SER   AAA CB  
776  O  OG  . SER   A 100 ? 0.838 0.406 0.706 0.243  -0.087 0.005  99  SER   AAA OG  
777  N  N   . THR   A 101 ? 0.593 0.302 0.503 0.269  0.075  0.121  100 THR   AAA N   
778  C  CA  . THR   A 101 ? 0.648 0.321 0.447 0.230  0.076  0.045  100 THR   AAA CA  
779  C  C   . THR   A 101 ? 0.516 0.237 0.448 0.132  0.019  -0.004 100 THR   AAA C   
780  O  O   . THR   A 101 ? 0.485 0.230 0.510 0.111  0.013  0.036  100 THR   AAA O   
781  C  CB  . THR   A 101 ? 0.635 0.422 0.451 0.286  0.006  -0.024 100 THR   AAA CB  
782  O  OG1 . THR   A 101 ? 0.797 0.226 0.552 0.208  -0.057 -0.041 100 THR   AAA OG1 
783  C  CG2 . THR   A 101 ? 0.725 0.427 0.543 0.229  0.122  0.086  100 THR   AAA CG2 
784  N  N   . ASN   A 102 ? 0.416 0.163 0.470 0.095  -0.031 -0.060 101 ASN   AAA N   
785  C  CA  . ASN   A 102 ? 0.434 0.179 0.422 0.090  -0.007 -0.059 101 ASN   AAA CA  
786  C  C   . ASN   A 102 ? 0.432 0.052 0.547 0.015  -0.032 0.010  101 ASN   AAA C   
787  O  O   . ASN   A 102 ? 0.421 0.031 0.469 0.020  0.004  -0.040 101 ASN   AAA O   
788  C  CB  . ASN   A 102 ? 0.463 0.042 0.581 0.042  -0.023 -0.062 101 ASN   AAA CB  
789  C  CG  . ASN   A 102 ? 0.373 0.208 0.451 -0.009 -0.009 -0.099 101 ASN   AAA CG  
790  O  OD1 . ASN   A 102 ? 0.524 0.126 0.465 0.059  -0.048 -0.128 101 ASN   AAA OD1 
791  N  ND2 . ASN   A 102 ? 0.366 0.106 0.536 0.023  0.000  -0.069 101 ASN   AAA ND2 
792  N  N   . GLU   A 103 ? 0.424 0.056 0.487 0.064  0.037  -0.022 102 GLU   AAA N   
793  C  CA  . GLU   A 103 ? 0.440 0.198 0.522 -0.010 0.002  -0.044 102 GLU   AAA CA  
794  C  C   . GLU   A 103 ? 0.464 0.137 0.497 0.061  0.007  -0.004 102 GLU   AAA C   
795  O  O   . GLU   A 103 ? 0.482 0.314 0.447 0.059  0.062  -0.093 102 GLU   AAA O   
796  C  CB  . GLU   A 103 ? 0.609 0.162 0.666 0.038  0.035  -0.033 102 GLU   AAA CB  
797  C  CG  . GLU   A 103 ? 0.808 0.383 0.632 -0.040 -0.143 -0.107 102 GLU   AAA CG  
798  C  CD  . GLU   A 103 ? 0.836 0.569 0.765 0.008  -0.043 -0.038 102 GLU   AAA CD  
799  O  OE1 . GLU   A 103 ? 0.600 0.689 0.777 0.139  -0.079 -0.111 102 GLU   AAA OE1 
800  O  OE2 . GLU   A 103 ? 1.169 0.319 1.083 0.012  -0.193 -0.150 102 GLU   AAA OE2 
801  N  N   . HIS   A 104 ? 0.434 0.009 0.539 0.036  0.013  0.004  103 HIS   AAA N   
802  C  CA  A HIS   A 104 ? 0.443 0.015 0.611 0.054  0.019  0.039  103 HIS   AAA CA  
803  C  CA  B HIS   A 104 ? 0.431 0.020 0.540 0.076  0.020  -0.009 103 HIS   AAA CA  
804  C  C   . HIS   A 104 ? 0.388 0.131 0.524 0.053  0.056  -0.149 103 HIS   AAA C   
805  O  O   . HIS   A 104 ? 0.482 0.048 0.551 0.051  -0.016 0.013  103 HIS   AAA O   
806  C  CB  A HIS   A 104 ? 0.522 0.009 0.671 0.037  0.037  -0.002 103 HIS   AAA CB  
807  C  CB  B HIS   A 104 ? 0.377 0.016 0.500 0.039  0.070  -0.046 103 HIS   AAA CB  
808  C  CG  A HIS   A 104 ? 0.563 0.012 0.707 0.030  0.022  0.056  103 HIS   AAA CG  
809  C  CG  B HIS   A 104 ? 0.396 0.077 0.516 0.063  0.007  0.010  103 HIS   AAA CG  
810  N  ND1 A HIS   A 104 ? 0.464 0.042 0.563 -0.119 -0.048 0.064  103 HIS   AAA ND1 
811  N  ND1 B HIS   A 104 ? 0.262 0.047 0.410 0.038  0.051  -0.070 103 HIS   AAA ND1 
812  C  CD2 A HIS   A 104 ? 0.585 0.008 0.631 0.018  -0.046 0.028  103 HIS   AAA CD2 
813  C  CD2 B HIS   A 104 ? 0.344 0.111 0.521 0.065  0.033  -0.054 103 HIS   AAA CD2 
814  C  CE1 A HIS   A 104 ? 0.465 0.032 0.558 -0.003 -0.056 0.033  103 HIS   AAA CE1 
815  C  CE1 B HIS   A 104 ? 0.239 0.158 0.514 0.155  -0.001 0.032  103 HIS   AAA CE1 
816  N  NE2 A HIS   A 104 ? 0.450 0.016 0.685 -0.051 -0.035 0.053  103 HIS   AAA NE2 
817  N  NE2 B HIS   A 104 ? 0.379 0.148 0.440 0.174  0.118  0.034  103 HIS   AAA NE2 
818  N  N   . GLY   A 105 ? 0.330 0.117 0.474 -0.030 -0.018 -0.119 104 GLY   AAA N   
819  C  CA  . GLY   A 105 ? 0.312 0.136 0.459 -0.004 -0.014 -0.120 104 GLY   AAA CA  
820  C  C   . GLY   A 105 ? 0.316 0.076 0.357 -0.049 -0.033 -0.071 104 GLY   AAA C   
821  O  O   . GLY   A 105 ? 0.362 0.008 0.476 0.020  0.019  -0.011 104 GLY   AAA O   
822  N  N   . SER   A 106 ? 0.304 0.035 0.352 -0.028 0.017  -0.054 105 SER   AAA N   
823  C  CA  . SER   A 106 ? 0.306 0.112 0.384 -0.016 -0.010 -0.072 105 SER   AAA CA  
824  C  C   . SER   A 106 ? 0.278 0.095 0.381 0.046  0.002  0.020  105 SER   AAA C   
825  O  O   . SER   A 106 ? 0.263 0.035 0.432 0.019  -0.003 -0.021 105 SER   AAA O   
826  C  CB  . SER   A 106 ? 0.296 0.049 0.364 -0.008 0.025  -0.068 105 SER   AAA CB  
827  O  OG  . SER   A 106 ? 0.331 0.054 0.365 0.052  0.008  -0.058 105 SER   AAA OG  
828  N  N   . GLU   A 107 ? 0.232 0.039 0.405 -0.006 -0.003 -0.003 106 GLU   AAA N   
829  C  CA  . GLU   A 107 ? 0.230 0.067 0.416 -0.008 0.006  -0.015 106 GLU   AAA CA  
830  C  C   . GLU   A 107 ? 0.319 0.041 0.404 0.006  -0.003 -0.045 106 GLU   AAA C   
831  O  O   . GLU   A 107 ? 0.362 0.032 0.405 0.002  0.030  -0.042 106 GLU   AAA O   
832  C  CB  . GLU   A 107 ? 0.252 0.008 0.406 -0.007 0.005  0.028  106 GLU   AAA CB  
833  C  CG  . GLU   A 107 ? 0.318 0.040 0.407 0.032  0.020  -0.022 106 GLU   AAA CG  
834  C  CD  . GLU   A 107 ? 0.276 0.045 0.366 0.100  -0.025 -0.032 106 GLU   AAA CD  
835  O  OE1 . GLU   A 107 ? 0.328 0.006 0.413 0.003  -0.008 -0.004 106 GLU   AAA OE1 
836  O  OE2 . GLU   A 107 ? 0.340 0.013 0.493 0.039  0.015  0.031  106 GLU   AAA OE2 
837  N  N   . HIS   A 108 ? 0.310 0.016 0.387 -0.006 0.010  -0.061 107 HIS   AAA N   
838  C  CA  . HIS   A 108 ? 0.337 0.013 0.349 0.026  0.040  -0.034 107 HIS   AAA CA  
839  C  C   . HIS   A 108 ? 0.278 0.092 0.341 -0.024 0.015  -0.077 107 HIS   AAA C   
840  O  O   . HIS   A 108 ? 0.281 0.028 0.424 -0.031 0.016  -0.017 107 HIS   AAA O   
841  C  CB  . HIS   A 108 ? 0.296 0.010 0.417 0.006  -0.007 -0.038 107 HIS   AAA CB  
842  C  CG  . HIS   A 108 ? 0.308 0.014 0.417 -0.007 0.015  -0.055 107 HIS   AAA CG  
843  N  ND1 . HIS   A 108 ? 0.297 0.045 0.373 -0.001 0.033  -0.053 107 HIS   AAA ND1 
844  C  CD2 . HIS   A 108 ? 0.337 0.058 0.389 -0.057 0.049  -0.106 107 HIS   AAA CD2 
845  C  CE1 . HIS   A 108 ? 0.322 0.036 0.448 0.032  0.041  -0.104 107 HIS   AAA CE1 
846  N  NE2 . HIS   A 108 ? 0.327 0.016 0.404 0.004  0.020  -0.060 107 HIS   AAA NE2 
847  N  N   . THR   A 109 ? 0.315 0.019 0.433 -0.025 0.025  -0.070 108 THR   AAA N   
848  C  CA  . THR   A 109 ? 0.336 0.023 0.458 -0.020 0.032  -0.085 108 THR   AAA CA  
849  C  C   . THR   A 109 ? 0.345 0.013 0.461 0.008  0.039  -0.052 108 THR   AAA C   
850  O  O   . THR   A 109 ? 0.344 0.021 0.472 -0.031 0.046  -0.077 108 THR   AAA O   
851  C  CB  . THR   A 109 ? 0.319 0.040 0.433 0.011  0.054  -0.023 108 THR   AAA CB  
852  O  OG1 . THR   A 109 ? 0.371 0.073 0.509 -0.026 0.062  -0.130 108 THR   AAA OG1 
853  C  CG2 . THR   A 109 ? 0.330 0.012 0.475 0.027  0.015  -0.023 108 THR   AAA CG2 
854  N  N   . VAL   A 110 ? 0.328 0.011 0.437 0.009  0.015  -0.041 109 VAL   AAA N   
855  C  CA  . VAL   A 110 ? 0.392 0.008 0.425 -0.023 0.024  -0.008 109 VAL   AAA CA  
856  C  C   . VAL   A 110 ? 0.330 0.136 0.394 0.023  0.000  -0.050 109 VAL   AAA C   
857  O  O   . VAL   A 110 ? 0.327 0.118 0.423 0.006  0.046  -0.067 109 VAL   AAA O   
858  C  CB  . VAL   A 110 ? 0.358 0.007 0.464 -0.004 0.025  -0.016 109 VAL   AAA CB  
859  C  CG1 . VAL   A 110 ? 0.408 0.047 0.446 0.038  0.047  -0.001 109 VAL   AAA CG1 
860  C  CG2 . VAL   A 110 ? 0.422 0.010 0.474 0.034  0.016  -0.015 109 VAL   AAA CG2 
861  N  N   . ASP   A 111 ? 0.380 0.116 0.429 -0.019 0.039  -0.055 110 ASP   AAA N   
862  C  CA  . ASP   A 111 ? 0.364 0.210 0.432 0.011  0.040  -0.093 110 ASP   AAA CA  
863  C  C   . ASP   A 111 ? 0.349 0.140 0.414 -0.029 0.054  -0.077 110 ASP   AAA C   
864  O  O   . ASP   A 111 ? 0.405 0.043 0.505 0.026  0.056  -0.032 110 ASP   AAA O   
865  C  CB  . ASP   A 111 ? 0.441 0.065 0.447 0.051  0.087  -0.081 110 ASP   AAA CB  
866  C  CG  . ASP   A 111 ? 0.355 0.211 0.431 -0.056 0.067  -0.027 110 ASP   AAA CG  
867  O  OD1 . ASP   A 111 ? 0.443 0.102 0.495 -0.079 0.061  -0.045 110 ASP   AAA OD1 
868  O  OD2 . ASP   A 111 ? 0.451 0.109 0.477 0.012  0.044  -0.058 110 ASP   AAA OD2 
869  N  N   . GLY   A 112 ? 0.397 0.089 0.403 -0.042 0.039  -0.057 111 GLY   AAA N   
870  C  CA  . GLY   A 112 ? 0.430 0.027 0.458 0.052  0.054  -0.030 111 GLY   AAA CA  
871  C  C   . GLY   A 112 ? 0.412 0.100 0.421 0.040  0.037  0.063  111 GLY   AAA C   
872  O  O   . GLY   A 112 ? 0.451 0.030 0.487 0.070  0.020  0.013  111 GLY   AAA O   
873  N  N   . VAL   A 113 ? 0.354 0.054 0.458 -0.032 0.053  -0.021 112 VAL   AAA N   
874  C  CA  . VAL   A 113 ? 0.311 0.122 0.446 0.009  0.064  -0.037 112 VAL   AAA CA  
875  C  C   . VAL   A 113 ? 0.272 0.152 0.415 -0.015 0.028  -0.030 112 VAL   AAA C   
876  O  O   . VAL   A 113 ? 0.324 0.074 0.487 0.014  0.014  -0.036 112 VAL   AAA O   
877  C  CB  . VAL   A 113 ? 0.378 0.165 0.446 -0.013 0.052  -0.015 112 VAL   AAA CB  
878  C  CG1 . VAL   A 113 ? 0.386 0.024 0.494 0.016  0.072  -0.064 112 VAL   AAA CG1 
879  C  CG2 . VAL   A 113 ? 0.401 0.107 0.441 -0.026 0.058  0.014  112 VAL   AAA CG2 
880  N  N   . LYS   A 114 ? 0.313 0.031 0.451 0.020  -0.000 -0.027 113 LYS   AAA N   
881  C  CA  . LYS   A 114 ? 0.358 0.027 0.461 -0.011 -0.006 -0.032 113 LYS   AAA CA  
882  C  C   . LYS   A 114 ? 0.270 0.021 0.495 0.037  0.005  -0.064 113 LYS   AAA C   
883  O  O   . LYS   A 114 ? 0.323 0.009 0.574 0.013  0.044  -0.036 113 LYS   AAA O   
884  C  CB  . LYS   A 114 ? 0.341 0.157 0.496 -0.013 -0.008 0.027  113 LYS   AAA CB  
885  C  CG  . LYS   A 114 ? 0.421 0.064 0.563 0.009  0.016  0.015  113 LYS   AAA CG  
886  C  CD  . LYS   A 114 ? 0.517 0.357 0.550 0.083  0.025  0.156  113 LYS   AAA CD  
887  C  CE  . LYS   A 114 ? 0.602 0.456 0.766 0.165  0.087  0.173  113 LYS   AAA CE  
888  N  NZ  . LYS   A 114 ? 0.718 0.541 0.938 0.037  0.125  0.350  113 LYS   AAA NZ  
889  N  N   . TYR   A 115 ? 0.295 0.018 0.414 0.031  0.015  -0.058 114 TYR   AAA N   
890  C  CA  . TYR   A 115 ? 0.305 0.047 0.414 0.003  0.000  -0.045 114 TYR   AAA CA  
891  C  C   . TYR   A 115 ? 0.282 0.116 0.415 -0.003 0.012  -0.059 114 TYR   AAA C   
892  O  O   . TYR   A 115 ? 0.327 0.088 0.444 0.014  0.007  -0.068 114 TYR   AAA O   
893  C  CB  . TYR   A 115 ? 0.325 0.036 0.391 -0.003 0.003  -0.027 114 TYR   AAA CB  
894  C  CG  . TYR   A 115 ? 0.358 0.012 0.393 0.004  0.038  -0.044 114 TYR   AAA CG  
895  C  CD1 . TYR   A 115 ? 0.400 0.118 0.370 -0.072 0.021  -0.021 114 TYR   AAA CD1 
896  C  CD2 . TYR   A 115 ? 0.311 0.056 0.399 0.030  -0.013 -0.002 114 TYR   AAA CD2 
897  C  CE1 . TYR   A 115 ? 0.401 0.206 0.373 -0.121 0.022  -0.032 114 TYR   AAA CE1 
898  C  CE2 . TYR   A 115 ? 0.390 0.046 0.423 0.001  -0.036 0.030  114 TYR   AAA CE2 
899  C  CZ  . TYR   A 115 ? 0.394 0.027 0.418 -0.036 -0.005 -0.037 114 TYR   AAA CZ  
900  O  OH  . TYR   A 115 ? 0.415 0.123 0.431 0.013  -0.002 -0.067 114 TYR   AAA OH  
901  N  N   . SER   A 116 ? 0.290 0.062 0.423 0.025  0.025  -0.056 115 SER   AAA N   
902  C  CA  . SER   A 116 ? 0.269 0.028 0.444 0.026  0.002  -0.027 115 SER   AAA CA  
903  C  C   . SER   A 116 ? 0.304 0.008 0.370 0.013  -0.027 -0.020 115 SER   AAA C   
904  O  O   . SER   A 116 ? 0.322 0.050 0.371 0.009  -0.012 -0.015 115 SER   AAA O   
905  C  CB  . SER   A 116 ? 0.240 0.103 0.440 0.004  0.012  -0.051 115 SER   AAA CB  
906  O  OG  . SER   A 116 ? 0.334 0.109 0.501 -0.005 0.063  -0.061 115 SER   AAA OG  
907  N  N   . ALA   A 117 ? 0.251 0.016 0.393 0.002  0.017  -0.000 116 ALA   AAA N   
908  C  CA  . ALA   A 117 ? 0.266 0.023 0.358 -0.007 0.016  0.005  116 ALA   AAA CA  
909  C  C   . ALA   A 117 ? 0.253 0.017 0.324 -0.041 0.015  0.009  116 ALA   AAA C   
910  O  O   . ALA   A 117 ? 0.298 0.011 0.347 0.033  0.019  -0.017 116 ALA   AAA O   
911  C  CB  . ALA   A 117 ? 0.269 0.096 0.418 -0.042 -0.007 -0.026 116 ALA   AAA CB  
912  N  N   . GLU   A 118 ? 0.261 0.038 0.353 -0.012 0.008  -0.017 117 GLU   AAA N   
913  C  CA  . GLU   A 118 ? 0.248 0.022 0.352 -0.034 -0.000 -0.055 117 GLU   AAA CA  
914  C  C   . GLU   A 118 ? 0.262 0.009 0.325 -0.006 -0.012 -0.029 117 GLU   AAA C   
915  O  O   . GLU   A 118 ? 0.357 0.012 0.356 0.029  -0.008 -0.037 117 GLU   AAA O   
916  C  CB  . GLU   A 118 ? 0.279 0.017 0.360 -0.031 0.001  -0.051 117 GLU   AAA CB  
917  C  CG  . GLU   A 118 ? 0.275 0.012 0.371 -0.035 -0.004 -0.020 117 GLU   AAA CG  
918  C  CD  . GLU   A 118 ? 0.227 0.022 0.412 -0.007 0.000  -0.056 117 GLU   AAA CD  
919  O  OE1 . GLU   A 118 ? 0.250 0.069 0.405 0.008  0.015  -0.016 117 GLU   AAA OE1 
920  O  OE2 . GLU   A 118 ? 0.308 0.047 0.389 0.054  0.020  -0.024 117 GLU   AAA OE2 
921  N  N   . LEU   A 119 ? 0.258 0.027 0.353 0.037  -0.008 -0.014 118 LEU   AAA N   
922  C  CA  . LEU   A 119 ? 0.274 0.011 0.376 -0.015 0.029  -0.040 118 LEU   AAA CA  
923  C  C   . LEU   A 119 ? 0.280 0.008 0.384 0.019  0.001  -0.002 118 LEU   AAA C   
924  O  O   . LEU   A 119 ? 0.273 0.007 0.390 0.014  -0.012 -0.012 118 LEU   AAA O   
925  C  CB  . LEU   A 119 ? 0.238 0.011 0.392 0.001  0.007  -0.005 118 LEU   AAA CB  
926  C  CG  . LEU   A 119 ? 0.248 0.076 0.342 0.050  0.024  0.024  118 LEU   AAA CG  
927  C  CD1 . LEU   A 119 ? 0.308 0.008 0.362 0.019  0.017  -0.008 118 LEU   AAA CD1 
928  C  CD2 . LEU   A 119 ? 0.307 0.109 0.349 0.039  0.058  0.024  118 LEU   AAA CD2 
929  N  N   . HIS   A 120 ? 0.348 0.009 0.426 0.023  0.010  -0.017 119 HIS   AAA N   
930  C  CA  . HIS   A 120 ? 0.337 0.018 0.414 0.027  0.003  -0.060 119 HIS   AAA CA  
931  C  C   . HIS   A 120 ? 0.331 0.017 0.400 0.054  -0.007 -0.028 119 HIS   AAA C   
932  O  O   . HIS   A 120 ? 0.348 0.017 0.419 0.061  0.008  0.003  119 HIS   AAA O   
933  C  CB  . HIS   A 120 ? 0.293 0.095 0.353 0.054  0.028  -0.047 119 HIS   AAA CB  
934  C  CG  . HIS   A 120 ? 0.297 0.063 0.353 0.023  -0.001 -0.032 119 HIS   AAA CG  
935  N  ND1 . HIS   A 120 ? 0.263 0.020 0.554 0.018  -0.072 -0.087 119 HIS   AAA ND1 
936  C  CD2 . HIS   A 120 ? 0.299 0.009 0.366 0.007  0.029  -0.031 119 HIS   AAA CD2 
937  C  CE1 . HIS   A 120 ? 0.290 0.039 0.288 -0.000 0.028  -0.093 119 HIS   AAA CE1 
938  N  NE2 . HIS   A 120 ? 0.291 0.011 0.318 0.005  0.007  -0.037 119 HIS   AAA NE2 
939  N  N   . VAL   A 121 ? 0.331 0.019 0.392 0.011  -0.021 -0.070 120 VAL   AAA N   
940  C  CA  . VAL   A 121 ? 0.279 0.021 0.412 0.024  -0.009 -0.072 120 VAL   AAA CA  
941  C  C   . VAL   A 121 ? 0.270 0.008 0.357 0.021  0.011  -0.000 120 VAL   AAA C   
942  O  O   . VAL   A 121 ? 0.284 0.013 0.376 0.040  -0.017 -0.019 120 VAL   AAA O   
943  C  CB  . VAL   A 121 ? 0.289 0.112 0.357 0.059  -0.007 -0.039 120 VAL   AAA CB  
944  C  CG1 . VAL   A 121 ? 0.322 0.044 0.382 0.006  0.007  -0.035 120 VAL   AAA CG1 
945  C  CG2 . VAL   A 121 ? 0.290 0.011 0.370 0.025  -0.000 0.028  120 VAL   AAA CG2 
946  N  N   . ALA   A 122 ? 0.265 0.014 0.390 0.036  0.005  -0.031 121 ALA   AAA N   
947  C  CA  . ALA   A 122 ? 0.253 0.022 0.355 0.042  0.009  -0.051 121 ALA   AAA CA  
948  C  C   . ALA   A 122 ? 0.242 0.078 0.406 0.066  -0.037 -0.060 121 ALA   AAA C   
949  O  O   . ALA   A 122 ? 0.277 0.057 0.377 0.005  -0.010 -0.027 121 ALA   AAA O   
950  C  CB  . ALA   A 122 ? 0.306 0.056 0.377 -0.015 -0.023 -0.044 121 ALA   AAA CB  
951  N  N   . HIS   A 123 ? 0.233 0.019 0.403 0.038  -0.013 -0.032 122 HIS   AAA N   
952  C  CA  . HIS   A 123 ? 0.205 0.068 0.401 0.052  0.010  -0.055 122 HIS   AAA CA  
953  C  C   . HIS   A 123 ? 0.230 0.090 0.429 0.009  0.006  -0.084 122 HIS   AAA C   
954  O  O   . HIS   A 123 ? 0.320 0.084 0.448 -0.008 -0.010 -0.073 122 HIS   AAA O   
955  C  CB  . HIS   A 123 ? 0.251 0.064 0.409 0.080  0.028  -0.051 122 HIS   AAA CB  
956  C  CG  . HIS   A 123 ? 0.255 0.008 0.405 0.001  0.014  -0.029 122 HIS   AAA CG  
957  N  ND1 . HIS   A 123 ? 0.280 0.151 0.374 0.060  0.047  -0.059 122 HIS   AAA ND1 
958  C  CD2 . HIS   A 123 ? 0.344 0.010 0.399 0.033  0.064  0.001  122 HIS   AAA CD2 
959  C  CE1 . HIS   A 123 ? 0.294 0.031 0.371 0.074  0.022  -0.039 122 HIS   AAA CE1 
960  N  NE2 . HIS   A 123 ? 0.303 0.010 0.381 -0.014 0.032  -0.037 122 HIS   AAA NE2 
961  N  N   . TRP   A 124 ? 0.247 0.109 0.428 0.040  0.009  -0.021 123 TRP   AAA N   
962  C  CA  . TRP   A 124 ? 0.269 0.024 0.461 0.037  0.023  -0.071 123 TRP   AAA CA  
963  C  C   . TRP   A 124 ? 0.198 0.163 0.453 0.010  0.016  -0.005 123 TRP   AAA C   
964  O  O   . TRP   A 124 ? 0.348 0.140 0.476 0.027  -0.002 -0.011 123 TRP   AAA O   
965  C  CB  . TRP   A 124 ? 0.306 0.029 0.446 0.018  0.009  -0.064 123 TRP   AAA CB  
966  C  CG  . TRP   A 124 ? 0.280 0.017 0.427 0.050  -0.002 -0.026 123 TRP   AAA CG  
967  C  CD1 . TRP   A 124 ? 0.288 0.088 0.419 0.044  -0.014 -0.039 123 TRP   AAA CD1 
968  C  CD2 . TRP   A 124 ? 0.292 0.012 0.411 0.038  0.030  0.011  123 TRP   AAA CD2 
969  N  NE1 . TRP   A 124 ? 0.306 0.081 0.433 0.002  -0.005 -0.062 123 TRP   AAA NE1 
970  C  CE2 . TRP   A 124 ? 0.312 0.018 0.453 0.021  -0.016 0.000  123 TRP   AAA CE2 
971  C  CE3 . TRP   A 124 ? 0.303 0.098 0.462 0.059  0.023  -0.010 123 TRP   AAA CE3 
972  C  CZ2 . TRP   A 124 ? 0.362 0.027 0.507 0.055  -0.006 0.028  123 TRP   AAA CZ2 
973  C  CZ3 . TRP   A 124 ? 0.271 0.096 0.501 0.060  0.033  0.016  123 TRP   AAA CZ3 
974  C  CH2 . TRP   A 124 ? 0.367 0.036 0.514 0.098  -0.002 0.038  123 TRP   AAA CH2 
975  N  N   . ASN   A 125 ? 0.220 0.200 0.433 -0.005 0.008  -0.010 124 ASN   AAA N   
976  C  CA  . ASN   A 125 ? 0.241 0.159 0.427 0.023  -0.017 -0.041 124 ASN   AAA CA  
977  C  C   . ASN   A 125 ? 0.298 0.102 0.474 -0.009 0.029  -0.043 124 ASN   AAA C   
978  O  O   . ASN   A 125 ? 0.314 0.082 0.459 0.029  0.027  0.019  124 ASN   AAA O   
979  C  CB  . ASN   A 125 ? 0.273 0.183 0.430 -0.011 -0.010 -0.041 124 ASN   AAA CB  
980  C  CG  . ASN   A 125 ? 0.302 0.251 0.452 0.075  -0.028 -0.090 124 ASN   AAA CG  
981  O  OD1 . ASN   A 125 ? 0.321 0.222 0.501 0.041  -0.023 -0.046 124 ASN   AAA OD1 
982  N  ND2 . ASN   A 125 ? 0.421 0.211 0.463 0.069  -0.042 -0.095 124 ASN   AAA ND2 
983  N  N   . SER   A 126 ? 0.280 0.079 0.468 0.026  -0.011 -0.000 125 SER   AAA N   
984  C  CA  . SER   A 126 ? 0.309 0.190 0.518 0.104  0.007  -0.011 125 SER   AAA CA  
985  C  C   . SER   A 126 ? 0.357 0.156 0.440 0.084  0.010  0.006  125 SER   AAA C   
986  O  O   . SER   A 126 ? 0.409 0.133 0.541 0.083  0.060  -0.000 125 SER   AAA O   
987  C  CB  . SER   A 126 ? 0.363 0.135 0.494 0.102  0.056  -0.037 125 SER   AAA CB  
988  O  OG  . SER   A 126 ? 0.367 0.279 0.490 0.030  0.039  -0.004 125 SER   AAA OG  
989  N  N   . ALA   A 127 ? 0.403 0.266 0.430 0.123  -0.020 0.027  126 ALA   AAA N   
990  C  CA  . ALA   A 127 ? 0.376 0.469 0.481 0.047  -0.004 0.054  126 ALA   AAA CA  
991  C  C   . ALA   A 127 ? 0.320 0.226 0.570 0.082  -0.006 -0.030 126 ALA   AAA C   
992  O  O   . ALA   A 127 ? 0.308 0.200 0.653 0.064  -0.006 0.000  126 ALA   AAA O   
993  C  CB  . ALA   A 127 ? 0.479 0.539 0.462 0.058  -0.015 0.069  126 ALA   AAA CB  
994  N  N   . LYS   A 128 ? 0.387 0.247 0.457 0.069  -0.009 -0.022 127 LYS   AAA N   
995  C  CA  . LYS   A 128 ? 0.355 0.165 0.478 0.101  0.010  -0.030 127 LYS   AAA CA  
996  C  C   . LYS   A 128 ? 0.277 0.188 0.485 0.086  0.006  -0.069 127 LYS   AAA C   
997  O  O   . LYS   A 128 ? 0.263 0.225 0.604 0.017  0.001  -0.050 127 LYS   AAA O   
998  C  CB  . LYS   A 128 ? 0.442 0.193 0.584 -0.034 0.078  -0.146 127 LYS   AAA CB  
999  C  CG  . LYS   A 128 ? 0.531 0.170 0.593 -0.015 0.067  -0.104 127 LYS   AAA CG  
1000 C  CD  . LYS   A 128 ? 0.652 0.145 0.777 -0.029 -0.030 -0.089 127 LYS   AAA CD  
1001 C  CE  . LYS   A 128 ? 0.573 0.304 0.820 0.043  0.029  -0.153 127 LYS   AAA CE  
1002 N  NZ  . LYS   A 128 ? 0.500 0.293 0.764 0.137  -0.156 -0.126 127 LYS   AAA NZ  
1003 N  N   . TYR   A 129 ? 0.293 0.127 0.556 -0.008 -0.013 -0.024 128 TYR   AAA N   
1004 C  CA  . TYR   A 129 ? 0.292 0.225 0.503 0.044  -0.021 -0.079 128 TYR   AAA CA  
1005 C  C   . TYR   A 129 ? 0.336 0.154 0.438 0.022  0.035  -0.003 128 TYR   AAA C   
1006 O  O   . TYR   A 129 ? 0.359 0.089 0.502 0.035  0.018  0.039  128 TYR   AAA O   
1007 C  CB  . TYR   A 129 ? 0.305 0.209 0.479 0.018  -0.015 -0.010 128 TYR   AAA CB  
1008 C  CG  . TYR   A 129 ? 0.288 0.253 0.431 0.047  -0.003 -0.045 128 TYR   AAA CG  
1009 C  CD1 . TYR   A 129 ? 0.286 0.244 0.533 0.061  0.021  -0.101 128 TYR   AAA CD1 
1010 C  CD2 . TYR   A 129 ? 0.276 0.190 0.434 0.000  0.010  -0.030 128 TYR   AAA CD2 
1011 C  CE1 . TYR   A 129 ? 0.384 0.310 0.424 0.066  -0.017 -0.097 128 TYR   AAA CE1 
1012 C  CE2 . TYR   A 129 ? 0.344 0.012 0.496 0.044  -0.005 -0.003 128 TYR   AAA CE2 
1013 C  CZ  . TYR   A 129 ? 0.360 0.334 0.402 -0.012 0.005  -0.081 128 TYR   AAA CZ  
1014 O  OH  . TYR   A 129 ? 0.313 0.204 0.504 -0.009 -0.048 -0.049 128 TYR   AAA OH  
1015 N  N   . SER   A 130 ? 0.351 0.149 0.421 0.059  -0.003 -0.042 129 SER   AAA N   
1016 C  CA  . SER   A 130 ? 0.453 0.210 0.421 0.092  -0.019 -0.117 129 SER   AAA CA  
1017 C  C   . SER   A 130 ? 0.396 0.161 0.464 0.122  -0.006 -0.158 129 SER   AAA C   
1018 O  O   . SER   A 130 ? 0.393 0.081 0.465 0.037  0.029  -0.054 129 SER   AAA O   
1019 C  CB  . SER   A 130 ? 0.636 0.150 0.513 0.189  0.098  -0.065 129 SER   AAA CB  
1020 O  OG  . SER   A 130 ? 0.612 0.344 0.589 0.003  -0.009 0.054  129 SER   AAA OG  
1021 N  N   . SER   A 131 ? 0.364 0.088 0.471 0.035  -0.010 -0.034 130 SER   AAA N   
1022 C  CA  . SER   A 131 ? 0.345 0.031 0.459 0.079  0.012  -0.049 130 SER   AAA CA  
1023 C  C   . SER   A 131 ? 0.340 0.013 0.437 0.047  0.006  -0.008 130 SER   AAA C   
1024 O  O   . SER   A 131 ? 0.338 0.101 0.450 0.032  0.001  -0.054 130 SER   AAA O   
1025 C  CB  . SER   A 131 ? 0.319 0.101 0.464 -0.010 -0.004 -0.024 130 SER   AAA CB  
1026 O  OG  . SER   A 131 ? 0.418 0.032 0.515 0.041  0.053  -0.042 130 SER   AAA OG  
1027 N  N   . LEU   A 132 ? 0.328 0.011 0.452 0.035  -0.001 -0.015 131 LEU   AAA N   
1028 C  CA  . LEU   A 132 ? 0.306 0.026 0.441 0.054  0.005  -0.003 131 LEU   AAA CA  
1029 C  C   . LEU   A 132 ? 0.380 0.089 0.366 -0.017 0.035  -0.025 131 LEU   AAA C   
1030 O  O   . LEU   A 132 ? 0.331 0.043 0.462 0.024  -0.002 -0.037 131 LEU   AAA O   
1031 C  CB  . LEU   A 132 ? 0.320 0.021 0.480 0.015  0.024  -0.046 131 LEU   AAA CB  
1032 C  CG  . LEU   A 132 ? 0.375 0.041 0.443 0.059  0.029  -0.014 131 LEU   AAA CG  
1033 C  CD1 . LEU   A 132 ? 0.319 0.052 0.451 0.017  -0.004 -0.032 131 LEU   AAA CD1 
1034 C  CD2 . LEU   A 132 ? 0.383 0.201 0.454 0.024  0.039  -0.073 131 LEU   AAA CD2 
1035 N  N   . ALA   A 133 ? 0.354 0.101 0.401 0.008  0.057  0.021  132 ALA   AAA N   
1036 C  CA  . ALA   A 133 ? 0.367 0.110 0.430 -0.003 0.038  0.040  132 ALA   AAA CA  
1037 C  C   . ALA   A 133 ? 0.345 0.008 0.545 -0.019 0.040  0.007  132 ALA   AAA C   
1038 O  O   . ALA   A 133 ? 0.468 0.015 0.543 -0.051 0.003  -0.038 132 ALA   AAA O   
1039 C  CB  . ALA   A 133 ? 0.424 0.113 0.453 -0.015 0.058  0.026  132 ALA   AAA CB  
1040 N  N   . GLU   A 134 ? 0.322 0.202 0.450 0.053  0.026  -0.018 133 GLU   AAA N   
1041 C  CA  . GLU   A 134 ? 0.314 0.164 0.456 0.048  0.016  -0.029 133 GLU   AAA CA  
1042 C  C   . GLU   A 134 ? 0.332 0.090 0.422 -0.052 0.014  -0.046 133 GLU   AAA C   
1043 O  O   . GLU   A 134 ? 0.384 0.053 0.498 -0.044 0.014  -0.041 133 GLU   AAA O   
1044 C  CB  . GLU   A 134 ? 0.349 0.117 0.426 0.042  0.033  0.000  133 GLU   AAA CB  
1045 C  CG  . GLU   A 134 ? 0.356 0.177 0.508 0.088  -0.020 -0.007 133 GLU   AAA CG  
1046 C  CD  . GLU   A 134 ? 0.301 0.163 0.553 0.077  -0.018 -0.074 133 GLU   AAA CD  
1047 O  OE1 . GLU   A 134 ? 0.365 0.129 0.570 0.018  0.044  0.036  133 GLU   AAA OE1 
1048 O  OE2 . GLU   A 134 ? 0.313 0.313 0.579 0.050  -0.015 -0.090 133 GLU   AAA OE2 
1049 N  N   . ALA   A 135 ? 0.293 0.060 0.436 0.019  0.003  -0.008 134 ALA   AAA N   
1050 C  CA  . ALA   A 135 ? 0.348 0.084 0.412 0.004  0.004  -0.009 134 ALA   AAA CA  
1051 C  C   . ALA   A 135 ? 0.314 0.093 0.410 -0.014 0.000  -0.005 134 ALA   AAA C   
1052 O  O   . ALA   A 135 ? 0.360 0.033 0.481 0.001  -0.017 -0.034 134 ALA   AAA O   
1053 C  CB  . ALA   A 135 ? 0.311 0.095 0.420 0.038  0.036  -0.012 134 ALA   AAA CB  
1054 N  N   . ALA   A 136 ? 0.294 0.070 0.428 0.038  -0.005 -0.030 135 ALA   AAA N   
1055 C  CA  . ALA   A 136 ? 0.297 0.119 0.464 0.050  -0.019 -0.029 135 ALA   AAA CA  
1056 C  C   . ALA   A 136 ? 0.317 0.153 0.428 0.022  0.048  -0.067 135 ALA   AAA C   
1057 O  O   . ALA   A 136 ? 0.365 0.123 0.478 0.076  0.042  -0.048 135 ALA   AAA O   
1058 C  CB  . ALA   A 136 ? 0.384 0.049 0.441 0.083  -0.002 -0.027 135 ALA   AAA CB  
1059 N  N   . SER   A 137 ? 0.320 0.077 0.500 0.007  0.032  -0.117 136 SER   AAA N   
1060 C  CA  . SER   A 137 ? 0.359 0.079 0.523 -0.016 0.048  -0.085 136 SER   AAA CA  
1061 C  C   . SER   A 137 ? 0.462 0.122 0.516 -0.042 0.005  -0.023 136 SER   AAA C   
1062 O  O   . SER   A 137 ? 0.499 0.118 0.682 -0.036 0.063  -0.125 136 SER   AAA O   
1063 C  CB  . SER   A 137 ? 0.391 0.103 0.569 -0.005 0.039  0.042  136 SER   AAA CB  
1064 O  OG  . SER   A 137 ? 0.369 0.161 0.577 -0.008 0.044  -0.037 136 SER   AAA OG  
1065 N  N   . LYS   A 138 ? 0.360 0.111 0.434 -0.048 0.033  -0.072 137 LYS   AAA N   
1066 C  CA  . LYS   A 138 ? 0.340 0.031 0.481 -0.058 0.009  -0.064 137 LYS   AAA CA  
1067 C  C   . LYS   A 138 ? 0.360 0.118 0.442 -0.050 -0.002 -0.080 137 LYS   AAA C   
1068 O  O   . LYS   A 138 ? 0.340 0.097 0.461 -0.013 -0.034 -0.088 137 LYS   AAA O   
1069 C  CB  . LYS   A 138 ? 0.344 0.127 0.515 0.037  0.024  -0.014 137 LYS   AAA CB  
1070 C  CG  . LYS   A 138 ? 0.386 0.268 0.528 0.034  0.063  -0.024 137 LYS   AAA CG  
1071 C  CD  . LYS   A 138 ? 0.416 0.458 0.579 -0.026 0.093  -0.032 137 LYS   AAA CD  
1072 C  CE  . LYS   A 138 ? 0.654 0.631 0.559 0.080  0.116  -0.138 137 LYS   AAA CE  
1073 N  NZ  . LYS   A 138 ? 0.747 0.715 0.641 0.230  0.201  -0.040 137 LYS   AAA NZ  
1074 N  N   . ALA   A 139 ? 0.344 0.128 0.470 -0.023 -0.045 -0.067 138 ALA   AAA N   
1075 C  CA  . ALA   A 139 ? 0.401 0.147 0.458 -0.031 -0.021 -0.055 138 ALA   AAA CA  
1076 C  C   . ALA   A 139 ? 0.292 0.152 0.468 -0.022 0.005  -0.086 138 ALA   AAA C   
1077 O  O   . ALA   A 139 ? 0.304 0.246 0.490 0.010  0.008  -0.059 138 ALA   AAA O   
1078 C  CB  . ALA   A 139 ? 0.356 0.273 0.575 -0.057 -0.022 -0.123 138 ALA   AAA CB  
1079 N  N   . ASP   A 140 ? 0.244 0.181 0.496 -0.008 0.007  -0.054 139 ASP   AAA N   
1080 C  CA  . ASP   A 140 ? 0.311 0.219 0.483 -0.019 0.020  -0.032 139 ASP   AAA CA  
1081 C  C   . ASP   A 140 ? 0.329 0.239 0.456 -0.021 -0.022 -0.016 139 ASP   AAA C   
1082 O  O   . ASP   A 140 ? 0.366 0.219 0.440 -0.020 -0.008 -0.013 139 ASP   AAA O   
1083 C  CB  . ASP   A 140 ? 0.327 0.238 0.548 -0.015 -0.024 -0.038 139 ASP   AAA CB  
1084 C  CG  . ASP   A 140 ? 0.379 0.188 0.488 -0.004 -0.015 -0.113 139 ASP   AAA CG  
1085 O  OD1 . ASP   A 140 ? 0.351 0.066 0.492 -0.001 0.001  -0.078 139 ASP   AAA OD1 
1086 O  OD2 . ASP   A 140 ? 0.387 0.402 0.544 0.044  -0.031 -0.096 139 ASP   AAA OD2 
1087 N  N   . GLY   A 141 ? 0.265 0.166 0.438 -0.001 -0.007 -0.052 140 GLY   AAA N   
1088 C  CA  . GLY   A 141 ? 0.268 0.154 0.450 0.026  0.001  -0.060 140 GLY   AAA CA  
1089 C  C   . GLY   A 141 ? 0.290 0.094 0.447 0.012  0.072  -0.025 140 GLY   AAA C   
1090 O  O   . GLY   A 141 ? 0.320 0.119 0.466 0.057  0.003  -0.066 140 GLY   AAA O   
1091 N  N   . LEU   A 142 ? 0.274 0.090 0.414 0.008  0.017  -0.075 141 LEU   AAA N   
1092 C  CA  . LEU   A 142 ? 0.295 0.034 0.437 -0.011 0.027  -0.045 141 LEU   AAA CA  
1093 C  C   . LEU   A 142 ? 0.274 0.109 0.429 -0.027 0.014  -0.048 141 LEU   AAA C   
1094 O  O   . LEU   A 142 ? 0.274 0.134 0.422 -0.024 -0.006 -0.022 141 LEU   AAA O   
1095 C  CB  . LEU   A 142 ? 0.324 0.025 0.445 -0.013 -0.005 -0.088 141 LEU   AAA CB  
1096 C  CG  . LEU   A 142 ? 0.269 0.027 0.457 -0.006 -0.009 -0.096 141 LEU   AAA CG  
1097 C  CD1 . LEU   A 142 ? 0.249 0.203 0.458 0.026  -0.013 -0.088 141 LEU   AAA CD1 
1098 C  CD2 . LEU   A 142 ? 0.328 0.010 0.418 -0.011 0.011  -0.036 141 LEU   AAA CD2 
1099 N  N   . ALA   A 143 ? 0.282 0.071 0.438 -0.028 0.013  -0.053 142 ALA   AAA N   
1100 C  CA  . ALA   A 143 ? 0.304 0.014 0.443 -0.011 0.014  -0.057 142 ALA   AAA CA  
1101 C  C   . ALA   A 143 ? 0.268 0.057 0.416 0.024  0.028  -0.085 142 ALA   AAA C   
1102 O  O   . ALA   A 143 ? 0.304 0.024 0.408 0.020  -0.016 -0.043 142 ALA   AAA O   
1103 C  CB  . ALA   A 143 ? 0.294 0.138 0.473 -0.003 -0.044 0.002  142 ALA   AAA CB  
1104 N  N   . VAL   A 144 ? 0.258 0.011 0.394 0.002  0.031  -0.038 143 VAL   AAA N   
1105 C  CA  . VAL   A 144 ? 0.268 0.063 0.336 0.039  -0.010 0.006  143 VAL   AAA CA  
1106 C  C   . VAL   A 144 ? 0.250 0.109 0.331 -0.060 -0.021 -0.020 143 VAL   AAA C   
1107 O  O   . VAL   A 144 ? 0.298 0.057 0.392 0.012  0.011  -0.056 143 VAL   AAA O   
1108 C  CB  . VAL   A 144 ? 0.311 0.007 0.380 -0.011 -0.022 0.010  143 VAL   AAA CB  
1109 C  CG1 . VAL   A 144 ? 0.297 0.017 0.422 0.013  -0.022 0.065  143 VAL   AAA CG1 
1110 C  CG2 . VAL   A 144 ? 0.268 0.026 0.427 -0.045 0.000  -0.025 143 VAL   AAA CG2 
1111 N  N   . ILE   A 145 ? 0.253 0.015 0.393 0.000  -0.008 -0.057 144 ILE   AAA N   
1112 C  CA  . ILE   A 145 ? 0.269 0.020 0.367 -0.033 -0.012 -0.057 144 ILE   AAA CA  
1113 C  C   . ILE   A 145 ? 0.284 0.088 0.321 0.003  0.015  -0.016 144 ILE   AAA C   
1114 O  O   . ILE   A 145 ? 0.330 0.022 0.346 0.054  0.003  -0.036 144 ILE   AAA O   
1115 C  CB  . ILE   A 145 ? 0.262 0.014 0.419 -0.036 -0.022 -0.032 144 ILE   AAA CB  
1116 C  CG1 . ILE   A 145 ? 0.287 0.008 0.412 -0.019 0.001  0.015  144 ILE   AAA CG1 
1117 C  CG2 . ILE   A 145 ? 0.323 0.038 0.453 0.006  0.021  0.002  144 ILE   AAA CG2 
1118 C  CD1 . ILE   A 145 ? 0.342 0.008 0.464 0.021  -0.004 -0.013 144 ILE   AAA CD1 
1119 N  N   . GLY   A 146 ? 0.267 0.100 0.359 -0.023 0.011  -0.049 145 GLY   AAA N   
1120 C  CA  . GLY   A 146 ? 0.296 0.022 0.393 0.001  0.010  -0.062 145 GLY   AAA CA  
1121 C  C   . GLY   A 146 ? 0.304 0.020 0.376 0.046  -0.009 -0.053 145 GLY   AAA C   
1122 O  O   . GLY   A 146 ? 0.304 0.032 0.377 -0.001 0.013  -0.031 145 GLY   AAA O   
1123 N  N   . VAL   A 147 ? 0.293 0.018 0.372 0.053  -0.015 -0.024 146 VAL   AAA N   
1124 C  CA  . VAL   A 147 ? 0.282 0.015 0.361 0.025  -0.016 -0.051 146 VAL   AAA CA  
1125 C  C   . VAL   A 147 ? 0.263 0.038 0.308 0.002  0.000  -0.000 146 VAL   AAA C   
1126 O  O   . VAL   A 147 ? 0.282 0.093 0.339 0.028  -0.034 -0.028 146 VAL   AAA O   
1127 C  CB  . VAL   A 147 ? 0.316 0.013 0.357 0.009  0.003  -0.043 146 VAL   AAA CB  
1128 C  CG1 . VAL   A 147 ? 0.318 0.013 0.409 0.046  0.022  -0.004 146 VAL   AAA CG1 
1129 C  CG2 . VAL   A 147 ? 0.322 0.068 0.417 0.027  -0.000 -0.020 146 VAL   AAA CG2 
1130 N  N   . LEU   A 148 ? 0.294 0.035 0.361 -0.036 0.016  -0.044 147 LEU   AAA N   
1131 C  CA  . LEU   A 148 ? 0.304 0.085 0.383 0.009  0.045  -0.001 147 LEU   AAA CA  
1132 C  C   . LEU   A 148 ? 0.288 0.111 0.310 0.023  0.004  -0.028 147 LEU   AAA C   
1133 O  O   . LEU   A 148 ? 0.309 0.131 0.337 0.031  0.016  -0.009 147 LEU   AAA O   
1134 C  CB  . LEU   A 148 ? 0.317 0.032 0.398 0.029  0.035  0.006  147 LEU   AAA CB  
1135 C  CG  . LEU   A 148 ? 0.409 0.100 0.441 -0.048 0.054  -0.026 147 LEU   AAA CG  
1136 C  CD1 . LEU   A 148 ? 0.398 0.228 0.458 -0.097 0.048  -0.057 147 LEU   AAA CD1 
1137 C  CD2 . LEU   A 148 ? 0.401 0.047 0.443 0.005  0.029  -0.056 147 LEU   AAA CD2 
1138 N  N   . MET   A 149 ? 0.297 0.006 0.358 -0.003 -0.008 0.001  148 MET   AAA N   
1139 C  CA  . MET   A 149 ? 0.263 0.020 0.382 0.014  0.039  0.006  148 MET   AAA CA  
1140 C  C   . MET   A 149 ? 0.257 0.086 0.354 0.040  0.019  0.006  148 MET   AAA C   
1141 O  O   . MET   A 149 ? 0.306 0.034 0.405 0.023  -0.005 -0.006 148 MET   AAA O   
1142 C  CB  . MET   A 149 ? 0.310 0.078 0.378 0.027  0.014  -0.010 148 MET   AAA CB  
1143 C  CG  . MET   A 149 ? 0.275 0.012 0.435 -0.026 0.022  0.036  148 MET   AAA CG  
1144 S  SD  . MET   A 149 ? 0.306 0.024 0.408 0.012  0.007  -0.012 148 MET   AAA SD  
1145 C  CE  . MET   A 149 ? 0.258 0.113 0.431 0.037  0.024  -0.020 148 MET   AAA CE  
1146 N  N   . LYS   A 150 ? 0.265 0.115 0.374 0.005  0.025  -0.036 149 LYS   AAA N   
1147 C  CA  A LYS   A 150 ? 0.267 0.117 0.402 -0.024 0.051  -0.055 149 LYS   AAA CA  
1148 C  CA  B LYS   A 150 ? 0.274 0.120 0.394 -0.013 0.043  -0.057 149 LYS   AAA CA  
1149 C  C   . LYS   A 150 ? 0.284 0.063 0.422 0.019  -0.001 -0.041 149 LYS   AAA C   
1150 O  O   . LYS   A 150 ? 0.279 0.065 0.439 0.002  0.025  -0.029 149 LYS   AAA O   
1151 C  CB  A LYS   A 150 ? 0.274 0.152 0.413 -0.055 0.039  -0.049 149 LYS   AAA CB  
1152 C  CB  B LYS   A 150 ? 0.313 0.155 0.402 -0.015 0.029  -0.051 149 LYS   AAA CB  
1153 C  CG  A LYS   A 150 ? 0.293 0.124 0.446 -0.094 0.074  -0.099 149 LYS   AAA CG  
1154 C  CG  B LYS   A 150 ? 0.360 0.149 0.418 -0.029 0.065  -0.093 149 LYS   AAA CG  
1155 C  CD  A LYS   A 150 ? 0.336 0.220 0.453 -0.094 0.052  -0.076 149 LYS   AAA CD  
1156 C  CD  B LYS   A 150 ? 0.438 0.245 0.422 -0.004 0.035  -0.046 149 LYS   AAA CD  
1157 C  CE  A LYS   A 150 ? 0.321 0.247 0.413 -0.107 0.124  -0.095 149 LYS   AAA CE  
1158 C  CE  B LYS   A 150 ? 0.555 0.278 0.377 0.084  0.059  -0.099 149 LYS   AAA CE  
1159 N  NZ  A LYS   A 150 ? 0.323 0.391 0.459 -0.089 0.131  -0.135 149 LYS   AAA NZ  
1160 N  NZ  B LYS   A 150 ? 0.677 0.329 0.439 0.157  -0.001 -0.010 149 LYS   AAA NZ  
1161 N  N   . VAL   A 151 ? 0.306 0.164 0.406 0.057  -0.003 -0.006 150 VAL   AAA N   
1162 C  CA  . VAL   A 151 ? 0.313 0.159 0.364 0.062  0.011  -0.078 150 VAL   AAA CA  
1163 C  C   . VAL   A 151 ? 0.297 0.109 0.361 0.026  -0.010 -0.037 150 VAL   AAA C   
1164 O  O   . VAL   A 151 ? 0.310 0.230 0.351 -0.014 0.028  -0.010 150 VAL   AAA O   
1165 C  CB  . VAL   A 151 ? 0.331 0.202 0.382 0.038  0.001  -0.016 150 VAL   AAA CB  
1166 C  CG1 . VAL   A 151 ? 0.353 0.230 0.413 0.041  0.058  -0.025 150 VAL   AAA CG1 
1167 C  CG2 . VAL   A 151 ? 0.357 0.172 0.459 0.048  -0.030 -0.036 150 VAL   AAA CG2 
1168 N  N   . GLY   A 152 ? 0.283 0.150 0.453 0.026  0.034  -0.105 151 GLY   AAA N   
1169 C  CA  . GLY   A 152 ? 0.303 0.205 0.443 -0.011 0.021  -0.063 151 GLY   AAA CA  
1170 C  C   . GLY   A 152 ? 0.350 0.218 0.403 -0.014 -0.032 -0.063 151 GLY   AAA C   
1171 O  O   . GLY   A 152 ? 0.322 0.320 0.428 -0.013 -0.028 -0.076 151 GLY   AAA O   
1172 N  N   . GLU   A 153 ? 0.355 0.222 0.446 0.027  0.013  -0.053 152 GLU   AAA N   
1173 C  CA  . GLU   A 153 ? 0.362 0.296 0.441 -0.053 -0.006 -0.081 152 GLU   AAA CA  
1174 C  C   . GLU   A 153 ? 0.337 0.311 0.437 -0.086 -0.007 -0.048 152 GLU   AAA C   
1175 O  O   . GLU   A 153 ? 0.341 0.181 0.463 -0.076 0.009  -0.041 152 GLU   AAA O   
1176 C  CB  . GLU   A 153 ? 0.497 0.289 0.464 -0.078 0.010  -0.045 152 GLU   AAA CB  
1177 C  CG  . GLU   A 153 ? 0.639 0.488 0.542 -0.140 0.065  -0.127 152 GLU   AAA CG  
1178 C  CD  . GLU   A 153 ? 0.711 0.578 0.898 -0.257 0.138  -0.042 152 GLU   AAA CD  
1179 O  OE1 . GLU   A 153 ? 0.930 0.775 0.854 -0.340 0.218  -0.176 152 GLU   AAA OE1 
1180 O  OE2 . GLU   A 153 ? 1.091 1.043 0.839 -0.380 0.117  0.036  152 GLU   AAA OE2 
1181 N  N   . ALA   A 154 ? 0.400 0.174 0.432 -0.089 0.005  -0.020 153 ALA   AAA N   
1182 C  CA  . ALA   A 154 ? 0.345 0.052 0.438 -0.059 0.003  -0.003 153 ALA   AAA CA  
1183 C  C   . ALA   A 154 ? 0.336 0.242 0.358 -0.016 -0.001 -0.008 153 ALA   AAA C   
1184 O  O   . ALA   A 154 ? 0.433 0.086 0.404 -0.018 0.040  -0.013 153 ALA   AAA O   
1185 C  CB  . ALA   A 154 ? 0.323 0.261 0.455 -0.093 0.010  -0.029 153 ALA   AAA CB  
1186 N  N   . ASN   A 155 ? 0.298 0.059 0.449 -0.009 0.008  -0.060 154 ASN   AAA N   
1187 C  CA  . ASN   A 155 ? 0.284 0.155 0.437 -0.022 -0.030 -0.062 154 ASN   AAA CA  
1188 C  C   . ASN   A 155 ? 0.325 0.096 0.444 -0.080 0.030  -0.038 154 ASN   AAA C   
1189 O  O   . ASN   A 155 ? 0.396 0.034 0.453 -0.083 0.035  -0.057 154 ASN   AAA O   
1190 C  CB  . ASN   A 155 ? 0.312 0.086 0.490 -0.011 -0.044 -0.078 154 ASN   AAA CB  
1191 C  CG  . ASN   A 155 ? 0.341 0.041 0.492 0.018  -0.055 -0.094 154 ASN   AAA CG  
1192 O  OD1 . ASN   A 155 ? 0.383 0.031 0.617 -0.006 -0.075 -0.055 154 ASN   AAA OD1 
1193 N  ND2 . ASN   A 155 ? 0.352 0.021 0.500 0.008  -0.009 -0.086 154 ASN   AAA ND2 
1194 N  N   . PRO   A 156 ? 0.393 0.108 0.475 -0.059 0.059  -0.003 155 PRO   AAA N   
1195 C  CA  . PRO   A 156 ? 0.419 0.152 0.495 -0.046 0.033  -0.052 155 PRO   AAA CA  
1196 C  C   . PRO   A 156 ? 0.377 0.194 0.430 -0.073 -0.009 0.017  155 PRO   AAA C   
1197 O  O   . PRO   A 156 ? 0.407 0.173 0.550 -0.044 0.050  -0.065 155 PRO   AAA O   
1198 C  CB  . PRO   A 156 ? 0.499 0.292 0.587 -0.099 0.045  0.022  155 PRO   AAA CB  
1199 C  CG  . PRO   A 156 ? 0.669 0.024 0.602 -0.093 0.115  0.006  155 PRO   AAA CG  
1200 C  CD  . PRO   A 156 ? 0.498 0.037 0.508 -0.095 0.092  0.018  155 PRO   AAA CD  
1201 N  N   . LYS   A 157 ? 0.405 0.208 0.424 -0.069 -0.013 0.028  156 LYS   AAA N   
1202 C  CA  . LYS   A 157 ? 0.433 0.189 0.438 -0.024 0.036  0.013  156 LYS   AAA CA  
1203 C  C   . LYS   A 157 ? 0.307 0.135 0.414 0.067  0.003  0.004  156 LYS   AAA C   
1204 O  O   . LYS   A 157 ? 0.387 0.171 0.493 -0.050 0.101  -0.080 156 LYS   AAA O   
1205 C  CB  . LYS   A 157 ? 0.413 0.277 0.439 0.081  0.035  -0.028 156 LYS   AAA CB  
1206 C  CG  . LYS   A 157 ? 0.447 0.381 0.477 0.060  0.079  -0.005 156 LYS   AAA CG  
1207 C  CD  . LYS   A 157 ? 0.624 0.427 0.651 0.098  0.062  0.064  156 LYS   AAA CD  
1208 C  CE  . LYS   A 157 ? 0.882 0.594 0.548 -0.027 0.130  0.036  156 LYS   AAA CE  
1209 N  NZ  . LYS   A 157 ? 0.868 0.670 0.676 0.066  0.218  0.077  156 LYS   AAA NZ  
1210 N  N   . LEU   A 158 ? 0.365 0.019 0.454 0.045  0.025  -0.021 157 LEU   AAA N   
1211 C  CA  . LEU   A 158 ? 0.372 0.148 0.455 0.032  0.059  -0.041 157 LEU   AAA CA  
1212 C  C   . LEU   A 158 ? 0.577 0.011 0.582 -0.049 0.015  0.009  157 LEU   AAA C   
1213 O  O   . LEU   A 158 ? 0.345 0.113 0.570 -0.001 0.005  0.053  157 LEU   AAA O   
1214 C  CB  . LEU   A 158 ? 0.344 0.127 0.476 -0.003 0.047  -0.038 157 LEU   AAA CB  
1215 C  CG  . LEU   A 158 ? 0.335 0.093 0.493 0.020  0.028  -0.058 157 LEU   AAA CG  
1216 C  CD1 . LEU   A 158 ? 0.334 0.116 0.528 0.041  0.012  -0.039 157 LEU   AAA CD1 
1217 C  CD2 . LEU   A 158 ? 0.383 0.148 0.625 0.024  0.068  -0.136 157 LEU   AAA CD2 
1218 N  N   . GLN   A 159 ? 0.390 0.030 0.580 -0.095 0.004  0.001  158 GLN   AAA N   
1219 C  CA  . GLN   A 159 ? 0.466 0.155 0.529 -0.060 -0.023 -0.016 158 GLN   AAA CA  
1220 C  C   . GLN   A 159 ? 0.447 0.075 0.566 0.008  -0.002 0.099  158 GLN   AAA C   
1221 O  O   . GLN   A 159 ? 0.441 0.316 0.516 -0.135 -0.035 0.126  158 GLN   AAA O   
1222 C  CB  . GLN   A 159 ? 0.397 0.267 0.562 -0.054 0.036  0.021  158 GLN   AAA CB  
1223 C  CG  . GLN   A 159 ? 0.401 0.405 0.572 -0.124 0.044  -0.033 158 GLN   AAA CG  
1224 C  CD  . GLN   A 159 ? 0.480 0.594 0.594 0.027  0.031  -0.036 158 GLN   AAA CD  
1225 O  OE1 . GLN   A 159 ? 0.668 0.500 0.675 -0.106 0.050  -0.191 158 GLN   AAA OE1 
1226 N  NE2 . GLN   A 159 ? 0.568 0.454 0.652 -0.017 -0.098 -0.046 158 GLN   AAA NE2 
1227 N  N   . LYS   A 160 ? 0.418 0.036 0.474 0.009  0.006  -0.037 159 LYS   AAA N   
1228 C  CA  . LYS   A 160 ? 0.359 0.116 0.440 -0.012 0.024  0.027  159 LYS   AAA CA  
1229 C  C   . LYS   A 160 ? 0.391 0.034 0.428 0.028  -0.032 0.011  159 LYS   AAA C   
1230 O  O   . LYS   A 160 ? 0.395 0.106 0.475 -0.030 -0.028 -0.047 159 LYS   AAA O   
1231 C  CB  . LYS   A 160 ? 0.516 0.011 0.598 0.039  0.033  -0.024 159 LYS   AAA CB  
1232 C  CG  . LYS   A 160 ? 0.544 0.146 0.589 -0.013 0.052  -0.071 159 LYS   AAA CG  
1233 C  CD  . LYS   A 160 ? 0.490 0.217 0.653 -0.023 0.042  -0.108 159 LYS   AAA CD  
1234 C  CE  . LYS   A 160 ? 0.498 0.106 0.611 -0.024 0.036  -0.082 159 LYS   AAA CE  
1235 N  NZ  . LYS   A 160 ? 0.596 0.361 0.674 -0.123 -0.005 -0.214 159 LYS   AAA NZ  
1236 N  N   . VAL   A 161 ? 0.386 0.042 0.484 0.007  -0.021 0.000  160 VAL   AAA N   
1237 C  CA  . VAL   A 161 ? 0.332 0.088 0.432 -0.023 -0.010 -0.011 160 VAL   AAA CA  
1238 C  C   . VAL   A 161 ? 0.298 0.024 0.409 -0.023 0.012  -0.080 160 VAL   AAA C   
1239 O  O   . VAL   A 161 ? 0.373 0.152 0.414 -0.006 0.034  -0.046 160 VAL   AAA O   
1240 C  CB  . VAL   A 161 ? 0.411 0.060 0.446 0.008  0.005  -0.041 160 VAL   AAA CB  
1241 C  CG1 . VAL   A 161 ? 0.546 0.154 0.493 -0.162 -0.043 0.001  160 VAL   AAA CG1 
1242 C  CG2 . VAL   A 161 ? 0.385 0.049 0.506 -0.005 0.010  -0.050 160 VAL   AAA CG2 
1243 N  N   . LEU   A 162 ? 0.294 0.148 0.462 0.026  0.025  -0.040 161 LEU   AAA N   
1244 C  CA  . LEU   A 162 ? 0.383 0.240 0.463 0.130  0.012  -0.040 161 LEU   AAA CA  
1245 C  C   . LEU   A 162 ? 0.322 0.208 0.417 0.079  0.021  -0.006 161 LEU   AAA C   
1246 O  O   . LEU   A 162 ? 0.358 0.201 0.416 0.111  0.008  -0.045 161 LEU   AAA O   
1247 C  CB  . LEU   A 162 ? 0.413 0.235 0.478 0.122  0.036  -0.003 161 LEU   AAA CB  
1248 C  CG  . LEU   A 162 ? 0.487 0.296 0.484 0.132  -0.003 -0.013 161 LEU   AAA CG  
1249 C  CD1 . LEU   A 162 ? 0.514 0.624 0.518 -0.022 0.047  0.012  161 LEU   AAA CD1 
1250 C  CD2 . LEU   A 162 ? 0.528 0.176 0.519 0.175  -0.048 -0.018 161 LEU   AAA CD2 
1251 N  N   . ASP   A 163 ? 0.317 0.228 0.518 -0.059 -0.014 -0.007 162 ASP   AAA N   
1252 C  CA  . ASP   A 163 ? 0.278 0.063 0.571 -0.099 0.010  0.020  162 ASP   AAA CA  
1253 C  C   . ASP   A 163 ? 0.298 0.112 0.480 -0.053 -0.052 0.053  162 ASP   AAA C   
1254 O  O   . ASP   A 163 ? 0.355 0.181 0.481 -0.050 -0.022 -0.013 162 ASP   AAA O   
1255 C  CB  . ASP   A 163 ? 0.361 0.080 0.580 -0.117 0.029  0.047  162 ASP   AAA CB  
1256 C  CG  . ASP   A 163 ? 0.363 0.249 0.593 -0.183 0.040  0.073  162 ASP   AAA CG  
1257 O  OD1 . ASP   A 163 ? 0.325 0.539 0.626 -0.075 0.055  0.071  162 ASP   AAA OD1 
1258 O  OD2 . ASP   A 163 ? 0.556 0.250 0.653 -0.139 0.116  0.073  162 ASP   AAA OD2 
1259 N  N   . ALA   A 164 ? 0.275 0.075 0.433 -0.007 -0.029 0.021  163 ALA   AAA N   
1260 C  CA  . ALA   A 164 ? 0.355 0.066 0.427 -0.065 0.009  0.006  163 ALA   AAA CA  
1261 C  C   . ALA   A 164 ? 0.346 0.059 0.389 -0.035 0.013  -0.018 163 ALA   AAA C   
1262 O  O   . ALA   A 164 ? 0.344 0.074 0.391 -0.034 -0.014 -0.018 163 ALA   AAA O   
1263 C  CB  . ALA   A 164 ? 0.369 0.034 0.439 -0.015 0.011  0.035  163 ALA   AAA CB  
1264 N  N   . LEU   A 165 ? 0.348 0.187 0.429 0.023  -0.007 -0.082 164 LEU   AAA N   
1265 C  CA  . LEU   A 165 ? 0.369 0.196 0.394 0.050  -0.015 -0.052 164 LEU   AAA CA  
1266 C  C   . LEU   A 165 ? 0.294 0.146 0.369 0.001  0.012  -0.063 164 LEU   AAA C   
1267 O  O   . LEU   A 165 ? 0.331 0.087 0.393 0.038  -0.008 -0.008 164 LEU   AAA O   
1268 C  CB  . LEU   A 165 ? 0.357 0.093 0.441 0.094  -0.048 -0.017 164 LEU   AAA CB  
1269 C  CG  . LEU   A 165 ? 0.378 0.028 0.426 0.071  -0.041 0.050  164 LEU   AAA CG  
1270 C  CD1 . LEU   A 165 ? 0.415 0.152 0.446 0.082  -0.004 -0.054 164 LEU   AAA CD1 
1271 C  CD2 . LEU   A 165 ? 0.392 0.133 0.414 0.006  0.015  0.017  164 LEU   AAA CD2 
1272 N  N   . GLN   A 166 ? 0.308 0.047 0.470 0.028  -0.036 -0.019 165 GLN   AAA N   
1273 C  CA  . GLN   A 166 ? 0.318 0.018 0.455 0.014  -0.031 -0.009 165 GLN   AAA CA  
1274 C  C   . GLN   A 166 ? 0.306 0.049 0.408 -0.056 -0.023 0.010  165 GLN   AAA C   
1275 O  O   . GLN   A 166 ? 0.398 0.066 0.425 0.046  -0.041 -0.022 165 GLN   AAA O   
1276 C  CB  . GLN   A 166 ? 0.295 0.222 0.574 -0.032 -0.055 -0.049 165 GLN   AAA CB  
1277 C  CG  . GLN   A 166 ? 0.410 0.263 0.635 -0.039 -0.062 -0.008 165 GLN   AAA CG  
1278 C  CD  . GLN   A 166 ? 0.570 0.105 0.667 -0.004 -0.053 0.002  165 GLN   AAA CD  
1279 O  OE1 . GLN   A 166 ? 0.579 0.256 0.665 -0.057 -0.092 -0.043 165 GLN   AAA OE1 
1280 N  NE2 . GLN   A 166 ? 0.477 0.394 0.985 0.112  -0.185 0.218  165 GLN   AAA NE2 
1281 N  N   . ALA   A 167 ? 0.354 0.147 0.418 -0.010 -0.031 -0.020 166 ALA   AAA N   
1282 C  CA  . ALA   A 167 ? 0.390 0.014 0.462 0.044  -0.007 -0.036 166 ALA   AAA CA  
1283 C  C   . ALA   A 167 ? 0.362 0.114 0.339 -0.002 -0.022 -0.064 166 ALA   AAA C   
1284 O  O   . ALA   A 167 ? 0.385 0.037 0.408 0.005  -0.011 -0.049 166 ALA   AAA O   
1285 C  CB  . ALA   A 167 ? 0.505 0.038 0.525 0.112  -0.034 -0.068 166 ALA   AAA CB  
1286 N  N   . ILE   A 168 ? 0.313 0.079 0.389 0.064  0.016  -0.067 167 ILE   AAA N   
1287 C  CA  . ILE   A 168 ? 0.300 0.108 0.425 0.057  0.003  -0.019 167 ILE   AAA CA  
1288 C  C   . ILE   A 168 ? 0.261 0.103 0.357 0.049  -0.020 -0.010 167 ILE   AAA C   
1289 O  O   . ILE   A 168 ? 0.318 0.144 0.425 0.017  -0.037 -0.040 167 ILE   AAA O   
1290 C  CB  . ILE   A 168 ? 0.316 0.062 0.433 0.071  0.001  0.005  167 ILE   AAA CB  
1291 C  CG1 . ILE   A 168 ? 0.299 0.088 0.433 0.055  -0.027 -0.045 167 ILE   AAA CG1 
1292 C  CG2 . ILE   A 168 ? 0.392 0.053 0.452 0.072  0.007  -0.058 167 ILE   AAA CG2 
1293 C  CD1 . ILE   A 168 ? 0.310 0.138 0.473 0.048  -0.079 -0.014 167 ILE   AAA CD1 
1294 N  N   . LYS   A 169 ? 0.267 0.049 0.405 0.027  -0.021 -0.049 168 LYS   AAA N   
1295 C  CA  . LYS   A 169 ? 0.292 0.076 0.424 0.059  -0.014 -0.047 168 LYS   AAA CA  
1296 C  C   . LYS   A 169 ? 0.283 0.120 0.391 0.009  0.020  -0.126 168 LYS   AAA C   
1297 O  O   . LYS   A 169 ? 0.324 0.013 0.407 0.014  0.012  -0.034 168 LYS   AAA O   
1298 C  CB  . LYS   A 169 ? 0.295 0.076 0.499 -0.005 -0.018 -0.028 168 LYS   AAA CB  
1299 C  CG  . LYS   A 169 ? 0.367 0.191 0.577 -0.055 -0.009 -0.009 168 LYS   AAA CG  
1300 C  CD  . LYS   A 169 ? 0.491 0.539 0.561 -0.030 -0.080 -0.139 168 LYS   AAA CD  
1301 C  CE  . LYS   A 169 ? 0.520 0.558 0.631 0.142  -0.058 -0.133 168 LYS   AAA CE  
1302 N  NZ  . LYS   A 169 ? 0.612 0.357 0.651 0.190  -0.203 -0.081 168 LYS   AAA NZ  
1303 N  N   . THR   A 170 ? 0.343 0.049 0.386 0.082  0.029  -0.039 169 THR   AAA N   
1304 C  CA  . THR   A 170 ? 0.339 0.025 0.425 0.026  -0.032 -0.039 169 THR   AAA CA  
1305 C  C   . THR   A 170 ? 0.328 0.083 0.416 -0.025 -0.000 -0.024 169 THR   AAA C   
1306 O  O   . THR   A 170 ? 0.296 0.122 0.432 -0.001 -0.002 -0.040 169 THR   AAA O   
1307 C  CB  . THR   A 170 ? 0.324 0.110 0.410 -0.003 -0.010 -0.051 169 THR   AAA CB  
1308 O  OG1 . THR   A 170 ? 0.333 0.139 0.403 0.082  -0.035 -0.057 169 THR   AAA OG1 
1309 C  CG2 . THR   A 170 ? 0.316 0.065 0.439 -0.005 -0.028 0.018  169 THR   AAA CG2 
1310 N  N   . LYS   A 171 ? 0.295 0.042 0.411 0.008  0.009  -0.048 170 LYS   AAA N   
1311 C  CA  . LYS   A 171 ? 0.306 0.111 0.421 -0.030 0.012  -0.068 170 LYS   AAA CA  
1312 C  C   . LYS   A 171 ? 0.333 0.060 0.372 -0.008 0.004  -0.002 170 LYS   AAA C   
1313 O  O   . LYS   A 171 ? 0.427 0.022 0.404 -0.007 -0.013 -0.008 170 LYS   AAA O   
1314 C  CB  . LYS   A 171 ? 0.354 0.114 0.423 -0.076 0.020  -0.090 170 LYS   AAA CB  
1315 C  CG  . LYS   A 171 ? 0.356 0.067 0.478 -0.059 0.034  -0.100 170 LYS   AAA CG  
1316 C  CD  . LYS   A 171 ? 0.428 0.090 0.552 -0.069 0.013  0.002  170 LYS   AAA CD  
1317 C  CE  . LYS   A 171 ? 0.478 0.308 0.676 -0.181 -0.020 -0.022 170 LYS   AAA CE  
1318 N  NZ  . LYS   A 171 ? 0.713 0.278 0.896 -0.144 0.011  0.016  170 LYS   AAA NZ  
1319 N  N   . GLY   A 172 ? 0.311 0.207 0.368 0.050  0.008  0.015  171 GLY   AAA N   
1320 C  CA  . GLY   A 172 ? 0.312 0.107 0.410 0.002  0.031  0.008  171 GLY   AAA CA  
1321 C  C   . GLY   A 172 ? 0.295 0.122 0.424 -0.008 0.041  0.024  171 GLY   AAA C   
1322 O  O   . GLY   A 172 ? 0.371 0.176 0.519 0.036  0.046  -0.036 171 GLY   AAA O   
1323 N  N   . LYS   A 173 ? 0.318 0.045 0.405 -0.014 0.024  0.031  172 LYS   AAA N   
1324 C  CA  . LYS   A 173 ? 0.331 0.042 0.376 -0.017 -0.001 0.022  172 LYS   AAA CA  
1325 C  C   . LYS   A 173 ? 0.346 0.092 0.353 0.018  -0.032 -0.034 172 LYS   AAA C   
1326 O  O   . LYS   A 173 ? 0.323 0.095 0.384 0.043  -0.022 -0.057 172 LYS   AAA O   
1327 C  CB  . LYS   A 173 ? 0.325 0.116 0.411 -0.011 0.009  -0.019 172 LYS   AAA CB  
1328 C  CG  . LYS   A 173 ? 0.332 0.147 0.400 0.002  0.028  -0.029 172 LYS   AAA CG  
1329 C  CD  . LYS   A 173 ? 0.347 0.162 0.430 -0.009 0.011  -0.048 172 LYS   AAA CD  
1330 C  CE  . LYS   A 173 ? 0.389 0.171 0.561 0.017  -0.004 -0.069 172 LYS   AAA CE  
1331 N  NZ  . LYS   A 173 ? 0.355 0.302 0.512 0.036  0.006  -0.073 172 LYS   AAA NZ  
1332 N  N   . ARG   A 174 ? 0.382 0.096 0.393 0.046  0.023  -0.013 173 ARG   AAA N   
1333 C  CA  . ARG   A 174 ? 0.344 0.027 0.385 -0.009 -0.047 -0.086 173 ARG   AAA CA  
1334 C  C   . ARG   A 174 ? 0.370 0.020 0.383 -0.049 -0.031 -0.047 173 ARG   AAA C   
1335 O  O   . ARG   A 174 ? 0.384 0.127 0.411 0.051  -0.070 -0.088 173 ARG   AAA O   
1336 C  CB  . ARG   A 174 ? 0.354 0.009 0.436 0.015  -0.022 -0.032 173 ARG   AAA CB  
1337 C  CG  . ARG   A 174 ? 0.406 0.145 0.447 0.013  0.003  -0.075 173 ARG   AAA CG  
1338 C  CD  . ARG   A 174 ? 0.386 0.185 0.464 0.081  0.042  -0.041 173 ARG   AAA CD  
1339 N  NE  . ARG   A 174 ? 0.491 0.255 0.490 -0.020 -0.061 0.078  173 ARG   AAA NE  
1340 C  CZ  . ARG   A 174 ? 0.476 0.311 0.590 -0.083 0.005  0.053  173 ARG   AAA CZ  
1341 N  NH1 . ARG   A 174 ? 0.432 0.257 0.683 -0.116 0.017  0.009  173 ARG   AAA NH1 
1342 N  NH2 . ARG   A 174 ? 0.419 0.366 0.692 -0.105 0.014  0.158  173 ARG   AAA NH2 
1343 N  N   . ALA   A 175 ? 0.329 0.018 0.425 0.023  -0.003 -0.065 174 ALA   AAA N   
1344 C  CA  . ALA   A 175 ? 0.360 0.055 0.417 -0.087 -0.021 -0.101 174 ALA   AAA CA  
1345 C  C   . ALA   A 175 ? 0.388 0.018 0.458 -0.039 -0.015 -0.056 174 ALA   AAA C   
1346 O  O   . ALA   A 175 ? 0.358 0.030 0.452 0.051  -0.012 -0.050 174 ALA   AAA O   
1347 C  CB  . ALA   A 175 ? 0.356 0.138 0.481 -0.083 -0.001 -0.110 174 ALA   AAA CB  
1348 N  N   . PRO   A 176 ? 0.443 0.023 0.485 -0.055 0.022  -0.068 175 PRO   AAA N   
1349 C  CA  . PRO   A 176 ? 0.464 0.029 0.526 -0.065 -0.017 -0.081 175 PRO   AAA CA  
1350 C  C   . PRO   A 176 ? 0.461 0.009 0.558 0.032  -0.003 0.003  175 PRO   AAA C   
1351 O  O   . PRO   A 176 ? 0.367 0.185 0.537 -0.009 0.003  -0.056 175 PRO   AAA O   
1352 C  CB  . PRO   A 176 ? 0.461 0.045 0.552 -0.008 -0.021 -0.144 175 PRO   AAA CB  
1353 C  CG  . PRO   A 176 ? 0.558 0.110 0.507 -0.069 0.018  -0.028 175 PRO   AAA CG  
1354 C  CD  . PRO   A 176 ? 0.455 0.138 0.439 0.008  0.008  -0.116 175 PRO   AAA CD  
1355 N  N   . PHE   A 177 ? 0.437 0.007 0.488 -0.019 0.031  0.007  176 PHE   AAA N   
1356 C  CA  . PHE   A 177 ? 0.401 0.011 0.473 -0.035 0.014  -0.031 176 PHE   AAA CA  
1357 C  C   . PHE   A 177 ? 0.353 0.018 0.446 -0.063 0.037  -0.004 176 PHE   AAA C   
1358 O  O   . PHE   A 177 ? 0.356 0.036 0.508 -0.007 0.017  -0.059 176 PHE   AAA O   
1359 C  CB  . PHE   A 177 ? 0.340 0.009 0.485 0.021  0.031  -0.020 176 PHE   AAA CB  
1360 C  CG  . PHE   A 177 ? 0.349 0.029 0.463 -0.021 0.017  -0.017 176 PHE   AAA CG  
1361 C  CD1 . PHE   A 177 ? 0.382 0.051 0.459 -0.039 -0.000 -0.008 176 PHE   AAA CD1 
1362 C  CD2 . PHE   A 177 ? 0.359 0.080 0.484 0.050  0.051  0.021  176 PHE   AAA CD2 
1363 C  CE1 . PHE   A 177 ? 0.376 0.047 0.491 -0.049 0.023  0.001  176 PHE   AAA CE1 
1364 C  CE2 . PHE   A 177 ? 0.345 0.130 0.489 0.056  0.038  0.029  176 PHE   AAA CE2 
1365 C  CZ  . PHE   A 177 ? 0.385 0.035 0.462 -0.029 0.041  -0.063 176 PHE   AAA CZ  
1366 N  N   . THR   A 178 ? 0.327 0.020 0.484 -0.066 0.020  -0.022 177 THR   AAA N   
1367 C  CA  . THR   A 178 ? 0.388 0.110 0.422 0.053  0.046  -0.072 177 THR   AAA CA  
1368 C  C   . THR   A 178 ? 0.372 0.019 0.397 -0.008 0.010  -0.071 177 THR   AAA C   
1369 O  O   . THR   A 178 ? 0.424 0.007 0.485 -0.001 0.037  -0.018 177 THR   AAA O   
1370 C  CB  . THR   A 178 ? 0.399 0.080 0.440 0.012  0.063  -0.060 177 THR   AAA CB  
1371 O  OG1 . THR   A 178 ? 0.468 0.101 0.486 -0.094 0.010  -0.023 177 THR   AAA OG1 
1372 C  CG2 . THR   A 178 ? 0.495 0.009 0.482 0.034  0.088  0.012  177 THR   AAA CG2 
1373 N  N   . ASN   A 179 ? 0.386 0.126 0.401 -0.014 0.015  -0.033 178 ASN   AAA N   
1374 C  CA  . ASN   A 179 ? 0.383 0.088 0.424 -0.015 0.047  -0.044 178 ASN   AAA CA  
1375 C  C   . ASN   A 179 ? 0.349 0.020 0.444 -0.052 0.030  -0.029 178 ASN   AAA C   
1376 O  O   . ASN   A 179 ? 0.391 0.094 0.479 -0.033 0.064  -0.042 178 ASN   AAA O   
1377 C  CB  . ASN   A 179 ? 0.448 0.053 0.416 -0.004 0.014  -0.058 178 ASN   AAA CB  
1378 C  CG  . ASN   A 179 ? 0.481 0.187 0.463 -0.046 0.098  0.019  178 ASN   AAA CG  
1379 O  OD1 . ASN   A 179 ? 0.589 0.011 0.599 0.052  0.056  0.011  178 ASN   AAA OD1 
1380 N  ND2 . ASN   A 179 ? 0.535 0.086 0.456 -0.071 0.079  -0.047 178 ASN   AAA ND2 
1381 N  N   . PHE   A 180 ? 0.428 0.025 0.467 -0.085 0.091  -0.045 179 PHE   AAA N   
1382 C  CA  . PHE   A 180 ? 0.373 0.113 0.395 0.009  0.062  -0.012 179 PHE   AAA CA  
1383 C  C   . PHE   A 180 ? 0.409 0.034 0.516 0.074  0.026  -0.079 179 PHE   AAA C   
1384 O  O   . PHE   A 180 ? 0.365 0.064 0.482 0.036  0.033  -0.027 179 PHE   AAA O   
1385 C  CB  . PHE   A 180 ? 0.419 0.070 0.386 0.011  0.054  -0.048 179 PHE   AAA CB  
1386 C  CG  . PHE   A 180 ? 0.379 0.041 0.452 -0.038 0.068  -0.079 179 PHE   AAA CG  
1387 C  CD1 . PHE   A 180 ? 0.367 0.137 0.436 -0.023 0.048  -0.056 179 PHE   AAA CD1 
1388 C  CD2 . PHE   A 180 ? 0.366 0.067 0.460 -0.073 0.058  -0.044 179 PHE   AAA CD2 
1389 C  CE1 . PHE   A 180 ? 0.363 0.107 0.529 -0.089 0.123  -0.083 179 PHE   AAA CE1 
1390 C  CE2 . PHE   A 180 ? 0.446 0.029 0.416 -0.020 0.091  0.025  179 PHE   AAA CE2 
1391 C  CZ  . PHE   A 180 ? 0.401 0.023 0.479 0.005  0.075  -0.087 179 PHE   AAA CZ  
1392 N  N   . ASP   A 181 ? 0.498 0.008 0.540 -0.006 0.002  -0.033 180 ASP   AAA N   
1393 C  CA  . ASP   A 181 ? 0.473 0.031 0.445 0.081  0.006  -0.033 180 ASP   AAA CA  
1394 C  C   . ASP   A 181 ? 0.417 0.010 0.505 -0.040 0.011  -0.008 180 ASP   AAA C   
1395 O  O   . ASP   A 181 ? 0.499 0.010 0.504 -0.040 0.058  -0.005 180 ASP   AAA O   
1396 C  CB  . ASP   A 181 ? 0.421 0.129 0.452 -0.046 -0.014 0.018  180 ASP   AAA CB  
1397 C  CG  . ASP   A 181 ? 0.492 0.053 0.423 -0.144 -0.000 0.036  180 ASP   AAA CG  
1398 O  OD1 . ASP   A 181 ? 0.379 0.007 0.530 0.013  0.053  -0.012 180 ASP   AAA OD1 
1399 O  OD2 . ASP   A 181 ? 0.541 0.149 0.522 0.027  0.034  0.092  180 ASP   AAA OD2 
1400 N  N   . PRO   A 182 ? 0.391 0.013 0.396 -0.041 0.089  -0.038 181 PRO   AAA N   
1401 C  CA  . PRO   A 182 ? 0.331 0.059 0.413 0.086  0.054  -0.029 181 PRO   AAA CA  
1402 C  C   . PRO   A 182 ? 0.333 0.103 0.394 0.019  0.027  -0.043 181 PRO   AAA C   
1403 O  O   . PRO   A 182 ? 0.416 0.006 0.469 -0.004 0.053  0.006  181 PRO   AAA O   
1404 C  CB  . PRO   A 182 ? 0.395 0.117 0.390 0.002  0.025  -0.045 181 PRO   AAA CB  
1405 C  CG  . PRO   A 182 ? 0.382 0.012 0.472 -0.044 0.049  -0.021 181 PRO   AAA CG  
1406 C  CD  . PRO   A 182 ? 0.347 0.008 0.435 -0.010 0.059  -0.027 181 PRO   AAA CD  
1407 N  N   . SER   A 183 ? 0.341 0.083 0.430 -0.001 0.006  -0.046 182 SER   AAA N   
1408 C  CA  . SER   A 183 ? 0.393 0.013 0.440 0.036  0.010  -0.038 182 SER   AAA CA  
1409 C  C   . SER   A 183 ? 0.392 0.012 0.382 0.044  0.000  -0.011 182 SER   AAA C   
1410 O  O   . SER   A 183 ? 0.434 0.030 0.425 0.017  0.055  -0.028 182 SER   AAA O   
1411 C  CB  . SER   A 183 ? 0.421 0.090 0.495 0.070  -0.016 -0.054 182 SER   AAA CB  
1412 O  OG  . SER   A 183 ? 0.575 0.068 0.446 0.051  -0.014 0.017  182 SER   AAA OG  
1413 N  N   . THR   A 184 ? 0.362 0.069 0.361 -0.001 0.017  -0.021 183 THR   AAA N   
1414 C  CA  . THR   A 184 ? 0.377 0.094 0.420 0.011  0.009  -0.024 183 THR   AAA CA  
1415 C  C   . THR   A 184 ? 0.329 0.057 0.397 -0.045 0.046  -0.018 183 THR   AAA C   
1416 O  O   . THR   A 184 ? 0.369 0.057 0.513 -0.057 0.094  -0.035 183 THR   AAA O   
1417 C  CB  . THR   A 184 ? 0.410 0.010 0.469 0.034  0.005  -0.014 183 THR   AAA CB  
1418 O  OG1 . THR   A 184 ? 0.443 0.014 0.454 -0.038 -0.004 -0.044 183 THR   AAA OG1 
1419 C  CG2 . THR   A 184 ? 0.447 0.007 0.481 -0.007 0.033  -0.008 183 THR   AAA CG2 
1420 N  N   . LEU   A 185 ? 0.338 0.008 0.400 -0.018 0.045  -0.020 184 LEU   AAA N   
1421 C  CA  . LEU   A 185 ? 0.372 0.064 0.372 0.059  0.012  -0.038 184 LEU   AAA CA  
1422 C  C   . LEU   A 185 ? 0.278 0.077 0.418 -0.013 0.011  -0.035 184 LEU   AAA C   
1423 O  O   . LEU   A 185 ? 0.383 0.087 0.460 0.027  -0.002 -0.110 184 LEU   AAA O   
1424 C  CB  . LEU   A 185 ? 0.319 0.028 0.393 0.022  0.032  -0.051 184 LEU   AAA CB  
1425 C  CG  . LEU   A 185 ? 0.380 0.033 0.397 0.055  0.018  -0.051 184 LEU   AAA CG  
1426 C  CD1 . LEU   A 185 ? 0.463 0.014 0.399 0.031  -0.002 -0.030 184 LEU   AAA CD1 
1427 C  CD2 . LEU   A 185 ? 0.383 0.034 0.455 -0.003 0.022  -0.036 184 LEU   AAA CD2 
1428 N  N   . LEU   A 186 ? 0.350 0.013 0.465 0.041  -0.015 -0.030 185 LEU   AAA N   
1429 C  CA  . LEU   A 186 ? 0.348 0.064 0.424 -0.032 0.010  -0.047 185 LEU   AAA CA  
1430 C  C   . LEU   A 186 ? 0.375 0.038 0.383 -0.003 0.020  -0.044 185 LEU   AAA C   
1431 O  O   . LEU   A 186 ? 0.358 0.051 0.468 0.009  0.020  -0.006 185 LEU   AAA O   
1432 C  CB  . LEU   A 186 ? 0.409 0.008 0.527 0.015  -0.007 -0.025 185 LEU   AAA CB  
1433 C  CG  . LEU   A 186 ? 0.408 0.017 0.500 0.066  0.008  0.002  185 LEU   AAA CG  
1434 C  CD1 . LEU   A 186 ? 0.343 0.111 0.499 0.024  -0.018 -0.080 185 LEU   AAA CD1 
1435 C  CD2 . LEU   A 186 ? 0.423 0.012 0.496 0.042  0.030  0.024  185 LEU   AAA CD2 
1436 N  N   . PRO   A 187 ? 0.345 0.009 0.438 0.011  0.028  -0.032 186 PRO   AAA N   
1437 C  CA  . PRO   A 187 ? 0.378 0.013 0.435 0.026  0.042  -0.044 186 PRO   AAA CA  
1438 C  C   . PRO   A 187 ? 0.431 0.192 0.384 0.064  0.029  -0.012 186 PRO   AAA C   
1439 O  O   . PRO   A 187 ? 0.426 0.016 0.455 -0.003 0.022  0.003  186 PRO   AAA O   
1440 C  CB  . PRO   A 187 ? 0.358 0.018 0.481 0.030  0.042  -0.056 186 PRO   AAA CB  
1441 C  CG  . PRO   A 187 ? 0.355 0.137 0.414 0.006  0.029  0.004  186 PRO   AAA CG  
1442 C  CD  . PRO   A 187 ? 0.354 0.009 0.401 0.009  0.008  0.031  186 PRO   AAA CD  
1443 N  N   . SER   A 188 ? 0.437 0.235 0.379 0.018  0.029  -0.027 187 SER   AAA N   
1444 C  CA  . SER   A 188 ? 0.459 0.263 0.445 -0.077 -0.007 0.038  187 SER   AAA CA  
1445 C  C   . SER   A 188 ? 0.379 0.131 0.483 0.029  -0.010 0.053  187 SER   AAA C   
1446 O  O   . SER   A 188 ? 0.469 0.235 0.620 0.124  -0.038 0.034  187 SER   AAA O   
1447 C  CB  . SER   A 188 ? 0.497 0.435 0.543 -0.205 0.044  0.127  187 SER   AAA CB  
1448 O  OG  . SER   A 188 ? 0.543 0.779 0.713 -0.022 0.024  0.155  187 SER   AAA OG  
1449 N  N   . SER   A 189 ? 0.401 0.115 0.576 -0.029 0.026  0.003  188 SER   AAA N   
1450 C  CA  . SER   A 189 ? 0.336 0.343 0.522 0.011  -0.002 0.022  188 SER   AAA CA  
1451 C  C   . SER   A 189 ? 0.360 0.100 0.482 -0.023 -0.006 -0.059 188 SER   AAA C   
1452 O  O   . SER   A 189 ? 0.413 0.102 0.476 0.005  0.017  0.009  188 SER   AAA O   
1453 C  CB  . SER   A 189 ? 0.415 0.377 0.479 -0.030 0.028  0.012  188 SER   AAA CB  
1454 O  OG  . SER   A 189 ? 0.422 0.397 0.452 0.021  -0.007 0.015  188 SER   AAA OG  
1455 N  N   . LEU   A 190 ? 0.369 0.119 0.549 0.017  -0.004 -0.049 189 LEU   AAA N   
1456 C  CA  . LEU   A 190 ? 0.392 0.189 0.495 0.049  0.005  -0.039 189 LEU   AAA CA  
1457 C  C   . LEU   A 190 ? 0.396 0.244 0.501 0.015  0.030  -0.056 189 LEU   AAA C   
1458 O  O   . LEU   A 190 ? 0.384 0.080 0.527 0.029  0.019  -0.004 189 LEU   AAA O   
1459 C  CB  . LEU   A 190 ? 0.385 0.124 0.579 0.010  0.016  -0.034 189 LEU   AAA CB  
1460 C  CG  . LEU   A 190 ? 0.419 0.342 0.499 0.097  -0.073 -0.101 189 LEU   AAA CG  
1461 C  CD1 . LEU   A 190 ? 0.499 0.290 0.545 0.171  -0.089 -0.060 189 LEU   AAA CD1 
1462 C  CD2 . LEU   A 190 ? 0.455 0.289 0.489 -0.011 -0.021 0.046  189 LEU   AAA CD2 
1463 N  N   . ASP   A 191 ? 0.390 0.206 0.457 -0.022 -0.005 -0.022 190 ASP   AAA N   
1464 C  CA  . ASP   A 191 ? 0.392 0.166 0.439 -0.033 0.018  0.007  190 ASP   AAA CA  
1465 C  C   . ASP   A 191 ? 0.376 0.197 0.363 0.024  0.010  -0.019 190 ASP   AAA C   
1466 O  O   . ASP   A 191 ? 0.338 0.146 0.439 0.038  -0.010 -0.052 190 ASP   AAA O   
1467 C  CB  . ASP   A 191 ? 0.413 0.139 0.460 -0.040 0.043  0.021  190 ASP   AAA CB  
1468 C  CG  . ASP   A 191 ? 0.434 0.269 0.490 0.001  0.014  0.087  190 ASP   AAA CG  
1469 O  OD1 . ASP   A 191 ? 0.483 0.334 0.514 0.033  -0.078 0.164  190 ASP   AAA OD1 
1470 O  OD2 . ASP   A 191 ? 0.622 0.250 0.492 -0.103 0.057  0.037  190 ASP   AAA OD2 
1471 N  N   . PHE   A 192 ? 0.364 0.175 0.378 0.038  0.004  -0.032 191 PHE   AAA N   
1472 C  CA  . PHE   A 192 ? 0.304 0.157 0.350 0.006  -0.043 -0.024 191 PHE   AAA CA  
1473 C  C   . PHE   A 192 ? 0.318 0.177 0.322 -0.017 -0.015 -0.031 191 PHE   AAA C   
1474 O  O   . PHE   A 192 ? 0.381 0.158 0.353 -0.005 -0.021 -0.008 191 PHE   AAA O   
1475 C  CB  . PHE   A 192 ? 0.309 0.211 0.367 0.013  -0.008 -0.009 191 PHE   AAA CB  
1476 C  CG  . PHE   A 192 ? 0.322 0.161 0.391 0.040  -0.009 -0.002 191 PHE   AAA CG  
1477 C  CD1 . PHE   A 192 ? 0.374 0.094 0.514 0.038  -0.001 0.010  191 PHE   AAA CD1 
1478 C  CD2 . PHE   A 192 ? 0.374 0.095 0.438 -0.010 -0.059 0.018  191 PHE   AAA CD2 
1479 C  CE1 . PHE   A 192 ? 0.346 0.109 0.525 0.048  0.042  -0.055 191 PHE   AAA CE1 
1480 C  CE2 . PHE   A 192 ? 0.388 0.108 0.433 0.028  -0.049 -0.017 191 PHE   AAA CE2 
1481 C  CZ  . PHE   A 192 ? 0.333 0.207 0.398 0.038  -0.029 0.047  191 PHE   AAA CZ  
1482 N  N   . TRP   A 193 ? 0.368 0.198 0.345 0.028  -0.008 -0.020 192 TRP   AAA N   
1483 C  CA  . TRP   A 193 ? 0.317 0.229 0.430 0.021  -0.013 -0.068 192 TRP   AAA CA  
1484 C  C   . TRP   A 193 ? 0.261 0.261 0.395 0.023  -0.070 -0.058 192 TRP   AAA C   
1485 O  O   . TRP   A 193 ? 0.305 0.292 0.365 -0.042 -0.002 -0.062 192 TRP   AAA O   
1486 C  CB  . TRP   A 193 ? 0.339 0.094 0.350 -0.065 0.013  -0.054 192 TRP   AAA CB  
1487 C  CG  . TRP   A 193 ? 0.323 0.058 0.420 0.023  0.006  -0.073 192 TRP   AAA CG  
1488 C  CD1 . TRP   A 193 ? 0.369 0.280 0.420 -0.017 -0.021 -0.096 192 TRP   AAA CD1 
1489 C  CD2 . TRP   A 193 ? 0.331 0.177 0.389 -0.031 0.001  -0.031 192 TRP   AAA CD2 
1490 N  NE1 . TRP   A 193 ? 0.420 0.138 0.418 -0.048 0.011  -0.101 192 TRP   AAA NE1 
1491 C  CE2 . TRP   A 193 ? 0.337 0.156 0.401 -0.040 0.028  -0.047 192 TRP   AAA CE2 
1492 C  CE3 . TRP   A 193 ? 0.327 0.088 0.397 -0.028 0.049  -0.090 192 TRP   AAA CE3 
1493 C  CZ2 . TRP   A 193 ? 0.352 0.148 0.381 -0.017 0.051  -0.097 192 TRP   AAA CZ2 
1494 C  CZ3 . TRP   A 193 ? 0.301 0.083 0.382 0.019  0.007  -0.051 192 TRP   AAA CZ3 
1495 C  CH2 . TRP   A 193 ? 0.292 0.124 0.405 0.018  0.033  -0.063 192 TRP   AAA CH2 
1496 N  N   . THR   A 194 ? 0.310 0.059 0.429 0.016  -0.021 -0.066 193 THR   AAA N   
1497 C  CA  . THR   A 194 ? 0.339 0.083 0.423 -0.028 0.001  -0.051 193 THR   AAA CA  
1498 C  C   . THR   A 194 ? 0.324 0.124 0.401 -0.057 0.010  -0.030 193 THR   AAA C   
1499 O  O   . THR   A 194 ? 0.315 0.124 0.468 -0.006 -0.003 -0.080 193 THR   AAA O   
1500 C  CB  . THR   A 194 ? 0.313 0.097 0.414 -0.043 0.002  -0.055 193 THR   AAA CB  
1501 O  OG1 . THR   A 194 ? 0.345 0.148 0.417 -0.015 0.027  -0.064 193 THR   AAA OG1 
1502 C  CG2 . THR   A 194 ? 0.326 0.108 0.457 -0.022 -0.023 -0.049 193 THR   AAA CG2 
1503 N  N   . TYR   A 195 ? 0.315 0.080 0.429 -0.024 0.002  -0.055 194 TYR   AAA N   
1504 C  CA  . TYR   A 195 ? 0.324 0.098 0.399 -0.049 -0.010 -0.089 194 TYR   AAA CA  
1505 C  C   . TYR   A 195 ? 0.283 0.199 0.401 -0.021 -0.019 -0.097 194 TYR   AAA C   
1506 O  O   . TYR   A 195 ? 0.306 0.062 0.409 0.004  -0.023 -0.068 194 TYR   AAA O   
1507 C  CB  . TYR   A 195 ? 0.335 0.070 0.447 -0.043 -0.033 -0.073 194 TYR   AAA CB  
1508 C  CG  . TYR   A 195 ? 0.327 0.098 0.423 -0.101 -0.023 -0.088 194 TYR   AAA CG  
1509 C  CD1 . TYR   A 195 ? 0.298 0.019 0.424 -0.048 -0.007 -0.044 194 TYR   AAA CD1 
1510 C  CD2 . TYR   A 195 ? 0.282 0.067 0.429 -0.046 0.031  -0.085 194 TYR   AAA CD2 
1511 C  CE1 . TYR   A 195 ? 0.278 0.069 0.443 -0.061 -0.020 -0.068 194 TYR   AAA CE1 
1512 C  CE2 . TYR   A 195 ? 0.292 0.036 0.493 -0.024 0.002  -0.050 194 TYR   AAA CE2 
1513 C  CZ  . TYR   A 195 ? 0.267 0.092 0.432 -0.025 0.003  -0.065 194 TYR   AAA CZ  
1514 O  OH  . TYR   A 195 ? 0.325 0.025 0.444 -0.064 -0.002 -0.044 194 TYR   AAA OH  
1515 N  N   . PRO   A 196 ? 0.351 0.049 0.475 -0.040 0.032  -0.105 195 PRO   AAA N   
1516 C  CA  . PRO   A 196 ? 0.348 0.071 0.461 -0.045 0.001  -0.090 195 PRO   AAA CA  
1517 C  C   . PRO   A 196 ? 0.378 0.080 0.460 0.040  -0.003 -0.128 195 PRO   AAA C   
1518 O  O   . PRO   A 196 ? 0.343 0.033 0.489 -0.028 0.009  -0.107 195 PRO   AAA O   
1519 C  CB  . PRO   A 196 ? 0.338 0.149 0.434 -0.049 0.002  -0.061 195 PRO   AAA CB  
1520 C  CG  . PRO   A 196 ? 0.357 0.164 0.467 -0.019 0.037  -0.092 195 PRO   AAA CG  
1521 C  CD  . PRO   A 196 ? 0.350 0.207 0.417 -0.035 0.023  -0.114 195 PRO   AAA CD  
1522 N  N   . GLY   A 197 ? 0.378 0.027 0.475 -0.044 0.011  -0.088 196 GLY   AAA N   
1523 C  CA  . GLY   A 197 ? 0.341 0.120 0.410 -0.057 -0.011 -0.065 196 GLY   AAA CA  
1524 C  C   . GLY   A 197 ? 0.313 0.012 0.450 -0.021 0.008  -0.042 196 GLY   AAA C   
1525 O  O   . GLY   A 197 ? 0.311 0.092 0.471 -0.034 0.019  -0.072 196 GLY   AAA O   
1526 N  N   . SER   A 198 ? 0.333 0.015 0.471 -0.017 0.012  -0.063 197 SER   AAA N   
1527 C  CA  . SER   A 198 ? 0.284 0.009 0.452 -0.014 0.046  -0.030 197 SER   AAA CA  
1528 C  C   . SER   A 198 ? 0.266 0.015 0.413 0.025  0.019  -0.049 197 SER   AAA C   
1529 O  O   . SER   A 198 ? 0.294 0.020 0.416 -0.002 0.018  -0.031 197 SER   AAA O   
1530 C  CB  . SER   A 198 ? 0.324 0.033 0.491 -0.092 0.024  -0.012 197 SER   AAA CB  
1531 O  OG  . SER   A 198 ? 0.372 0.025 0.521 -0.055 0.081  -0.084 197 SER   AAA OG  
1532 N  N   . LEU   A 199 ? 0.299 0.075 0.409 -0.007 0.013  -0.039 198 LEU   AAA N   
1533 C  CA  . LEU   A 199 ? 0.258 0.065 0.392 0.030  0.003  -0.034 198 LEU   AAA CA  
1534 C  C   . LEU   A 199 ? 0.252 0.013 0.434 -0.016 -0.003 -0.047 198 LEU   AAA C   
1535 O  O   . LEU   A 199 ? 0.337 0.013 0.398 -0.030 0.036  -0.044 198 LEU   AAA O   
1536 C  CB  . LEU   A 199 ? 0.365 0.045 0.397 0.022  0.004  -0.060 198 LEU   AAA CB  
1537 C  CG  . LEU   A 199 ? 0.324 0.007 0.430 -0.015 0.024  0.005  198 LEU   AAA CG  
1538 C  CD1 . LEU   A 199 ? 0.363 0.022 0.484 -0.008 0.030  -0.087 198 LEU   AAA CD1 
1539 C  CD2 . LEU   A 199 ? 0.381 0.009 0.473 0.026  0.055  -0.018 198 LEU   AAA CD2 
1540 N  N   . THR   A 200 ? 0.238 0.031 0.434 0.014  0.049  -0.055 199 THR   AAA N   
1541 C  CA  . THR   A 200 ? 0.293 0.012 0.401 0.016  0.013  -0.045 199 THR   AAA CA  
1542 C  C   . THR   A 200 ? 0.260 0.065 0.388 -0.051 0.051  -0.037 199 THR   AAA C   
1543 O  O   . THR   A 200 ? 0.316 0.050 0.459 -0.006 0.031  -0.020 199 THR   AAA O   
1544 C  CB  . THR   A 200 ? 0.320 0.084 0.411 -0.012 0.031  -0.070 199 THR   AAA CB  
1545 O  OG1 . THR   A 200 ? 0.358 0.013 0.393 0.047  -0.009 -0.010 199 THR   AAA OG1 
1546 C  CG2 . THR   A 200 ? 0.392 0.012 0.433 -0.015 0.036  -0.047 199 THR   AAA CG2 
1547 N  N   . HIS   A 201 ? 0.299 0.034 0.401 -0.019 0.036  -0.050 200 HIS   AAA N   
1548 C  CA  . HIS   A 201 ? 0.332 0.011 0.436 0.029  0.037  -0.023 200 HIS   AAA CA  
1549 C  C   . HIS   A 201 ? 0.319 0.011 0.402 -0.027 0.033  -0.034 200 HIS   AAA C   
1550 O  O   . HIS   A 201 ? 0.325 0.041 0.432 -0.007 0.022  -0.044 200 HIS   AAA O   
1551 C  CB  . HIS   A 201 ? 0.378 0.023 0.446 0.067  -0.011 0.043  200 HIS   AAA CB  
1552 C  CG  . HIS   A 201 ? 0.369 0.009 0.418 0.013  0.006  0.028  200 HIS   AAA CG  
1553 N  ND1 . HIS   A 201 ? 0.429 0.013 0.544 0.011  0.065  -0.058 200 HIS   AAA ND1 
1554 C  CD2 . HIS   A 201 ? 0.262 0.014 0.430 -0.034 0.032  0.035  200 HIS   AAA CD2 
1555 C  CE1 . HIS   A 201 ? 0.331 0.011 0.489 0.034  -0.003 -0.027 200 HIS   AAA CE1 
1556 N  NE2 . HIS   A 201 ? 0.413 0.023 0.536 -0.081 0.015  -0.020 200 HIS   AAA NE2 
1557 N  N   . PRO   A 202 ? 0.357 0.025 0.400 0.021  0.015  -0.016 201 PRO   AAA N   
1558 C  CA  . PRO   A 202 ? 0.379 0.008 0.425 0.003  0.059  -0.028 201 PRO   AAA CA  
1559 C  C   . PRO   A 202 ? 0.340 0.033 0.467 0.080  0.040  -0.049 201 PRO   AAA C   
1560 O  O   . PRO   A 202 ? 0.375 0.051 0.437 0.056  0.018  -0.031 201 PRO   AAA O   
1561 C  CB  . PRO   A 202 ? 0.325 0.071 0.426 0.017  0.064  -0.008 201 PRO   AAA CB  
1562 C  CG  . PRO   A 202 ? 0.348 0.049 0.489 0.011  0.067  -0.026 201 PRO   AAA CG  
1563 C  CD  . PRO   A 202 ? 0.348 0.112 0.414 0.053  0.047  0.019  201 PRO   AAA CD  
1564 N  N   . PRO   A 203 ? 0.327 0.023 0.434 0.027  0.025  -0.077 202 PRO   AAA N   
1565 C  CA  . PRO   A 203 ? 0.355 0.062 0.436 -0.040 0.041  -0.039 202 PRO   AAA CA  
1566 C  C   . PRO   A 203 ? 0.306 0.045 0.442 0.001  0.044  -0.034 202 PRO   AAA C   
1567 O  O   . PRO   A 203 ? 0.346 0.010 0.525 -0.016 0.046  -0.002 202 PRO   AAA O   
1568 C  CB  . PRO   A 203 ? 0.392 0.011 0.489 -0.013 0.008  -0.048 202 PRO   AAA CB  
1569 C  CG  . PRO   A 203 ? 0.404 0.015 0.473 -0.001 0.017  -0.063 202 PRO   AAA CG  
1570 C  CD  . PRO   A 203 ? 0.407 0.023 0.452 0.049  -0.000 -0.069 202 PRO   AAA CD  
1571 N  N   . LEU   A 204 ? 0.327 0.038 0.451 -0.043 0.059  -0.066 203 LEU   AAA N   
1572 C  CA  . LEU   A 204 ? 0.382 0.014 0.456 0.048  0.004  -0.028 203 LEU   AAA CA  
1573 C  C   . LEU   A 204 ? 0.344 0.089 0.458 0.109  0.029  -0.060 203 LEU   AAA C   
1574 O  O   . LEU   A 204 ? 0.353 0.008 0.502 -0.005 0.063  -0.030 203 LEU   AAA O   
1575 C  CB  . LEU   A 204 ? 0.363 0.012 0.466 -0.009 0.075  -0.049 203 LEU   AAA CB  
1576 C  CG  . LEU   A 204 ? 0.416 0.015 0.573 -0.058 0.035  0.000  203 LEU   AAA CG  
1577 C  CD1 . LEU   A 204 ? 0.417 0.014 0.619 -0.053 0.086  0.007  203 LEU   AAA CD1 
1578 C  CD2 . LEU   A 204 ? 0.428 0.013 0.514 -0.051 0.032  -0.024 203 LEU   AAA CD2 
1579 N  N   . TYR   A 205 ? 0.361 0.007 0.501 -0.006 0.031  -0.008 204 TYR   AAA N   
1580 C  CA  . TYR   A 205 ? 0.327 0.017 0.458 0.017  0.065  -0.061 204 TYR   AAA CA  
1581 C  C   . TYR   A 205 ? 0.257 0.067 0.451 0.016  0.058  -0.094 204 TYR   AAA C   
1582 O  O   . TYR   A 205 ? 0.307 0.019 0.463 -0.015 0.055  -0.072 204 TYR   AAA O   
1583 C  CB  . TYR   A 205 ? 0.295 0.013 0.485 -0.038 0.077  -0.036 204 TYR   AAA CB  
1584 C  CG  . TYR   A 205 ? 0.393 0.011 0.495 0.004  0.079  -0.044 204 TYR   AAA CG  
1585 C  CD1 . TYR   A 205 ? 0.508 0.131 0.497 -0.099 0.089  -0.009 204 TYR   AAA CD1 
1586 C  CD2 . TYR   A 205 ? 0.314 0.146 0.454 -0.051 0.011  -0.108 204 TYR   AAA CD2 
1587 C  CE1 . TYR   A 205 ? 0.647 0.194 0.584 -0.073 0.134  -0.128 204 TYR   AAA CE1 
1588 C  CE2 . TYR   A 205 ? 0.377 0.039 0.511 0.064  0.087  -0.027 204 TYR   AAA CE2 
1589 C  CZ  . TYR   A 205 ? 0.586 0.121 0.534 -0.138 0.022  0.019  204 TYR   AAA CZ  
1590 O  OH  . TYR   A 205 ? 0.603 0.561 0.569 -0.068 0.018  -0.038 204 TYR   AAA OH  
1591 N  N   . GLU   A 206 ? 0.330 0.022 0.509 -0.065 0.038  -0.043 205 GLU   AAA N   
1592 C  CA  . GLU   A 206 ? 0.352 0.051 0.474 -0.017 0.052  -0.069 205 GLU   AAA CA  
1593 C  C   . GLU   A 206 ? 0.261 0.055 0.456 -0.085 -0.000 -0.077 205 GLU   AAA C   
1594 O  O   . GLU   A 206 ? 0.291 0.049 0.532 -0.043 -0.028 -0.073 205 GLU   AAA O   
1595 C  CB  . GLU   A 206 ? 0.351 0.130 0.510 -0.060 0.019  -0.108 205 GLU   AAA CB  
1596 C  CG  . GLU   A 206 ? 0.382 0.146 0.511 -0.042 0.023  -0.066 205 GLU   AAA CG  
1597 C  CD  . GLU   A 206 ? 0.370 0.163 0.517 -0.056 0.025  -0.070 205 GLU   AAA CD  
1598 O  OE1 . GLU   A 206 ? 0.455 0.020 0.628 -0.067 0.074  -0.056 205 GLU   AAA OE1 
1599 O  OE2 . GLU   A 206 ? 0.382 0.222 0.542 -0.060 0.013  -0.070 205 GLU   AAA OE2 
1600 N  N   . SER   A 207 ? 0.250 0.037 0.506 -0.051 -0.000 -0.099 206 SER   AAA N   
1601 C  CA  . SER   A 207 ? 0.269 0.128 0.431 0.034  0.021  -0.051 206 SER   AAA CA  
1602 C  C   . SER   A 207 ? 0.323 0.021 0.460 0.021  0.023  -0.076 206 SER   AAA C   
1603 O  O   . SER   A 207 ? 0.337 0.015 0.521 0.036  0.018  -0.045 206 SER   AAA O   
1604 C  CB  . SER   A 207 ? 0.351 0.029 0.483 0.082  -0.031 -0.046 206 SER   AAA CB  
1605 O  OG  . SER   A 207 ? 0.382 0.069 0.454 -0.039 -0.009 -0.026 206 SER   AAA OG  
1606 N  N   . VAL   A 208 ? 0.245 0.016 0.450 -0.027 0.034  -0.059 207 VAL   AAA N   
1607 C  CA  . VAL   A 208 ? 0.241 0.040 0.427 -0.029 0.040  -0.074 207 VAL   AAA CA  
1608 C  C   . VAL   A 208 ? 0.349 0.060 0.413 -0.024 -0.017 -0.027 207 VAL   AAA C   
1609 O  O   . VAL   A 208 ? 0.336 0.138 0.494 -0.066 0.023  -0.148 207 VAL   AAA O   
1610 C  CB  . VAL   A 208 ? 0.286 0.008 0.399 -0.012 -0.025 -0.019 207 VAL   AAA CB  
1611 C  CG1 . VAL   A 208 ? 0.275 0.013 0.465 -0.009 0.020  -0.056 207 VAL   AAA CG1 
1612 C  CG2 . VAL   A 208 ? 0.282 0.019 0.413 0.020  -0.003 -0.017 207 VAL   AAA CG2 
1613 N  N   . THR   A 209 ? 0.374 0.061 0.421 0.002  -0.021 -0.041 208 THR   AAA N   
1614 C  CA  . THR   A 209 ? 0.316 0.010 0.428 0.002  0.001  -0.041 208 THR   AAA CA  
1615 C  C   . THR   A 209 ? 0.305 0.115 0.383 -0.010 0.018  -0.102 208 THR   AAA C   
1616 O  O   . THR   A 209 ? 0.262 0.083 0.469 -0.018 -0.007 -0.059 208 THR   AAA O   
1617 C  CB  . THR   A 209 ? 0.274 0.187 0.463 0.030  -0.032 -0.006 208 THR   AAA CB  
1618 O  OG1 . THR   A 209 ? 0.304 0.264 0.471 -0.041 0.023  -0.076 208 THR   AAA OG1 
1619 C  CG2 . THR   A 209 ? 0.364 0.293 0.473 0.069  -0.047 -0.003 208 THR   AAA CG2 
1620 N  N   . TRP   A 210 ? 0.321 0.031 0.393 0.016  -0.014 -0.072 209 TRP   AAA N   
1621 C  CA  . TRP   A 210 ? 0.329 0.069 0.376 0.020  0.012  -0.096 209 TRP   AAA CA  
1622 C  C   . TRP   A 210 ? 0.315 0.013 0.402 0.037  -0.064 -0.036 209 TRP   AAA C   
1623 O  O   . TRP   A 210 ? 0.323 0.099 0.405 0.043  -0.046 -0.027 209 TRP   AAA O   
1624 C  CB  . TRP   A 210 ? 0.321 0.033 0.405 -0.020 0.010  -0.098 209 TRP   AAA CB  
1625 C  CG  . TRP   A 210 ? 0.257 0.057 0.419 0.010  0.010  -0.104 209 TRP   AAA CG  
1626 C  CD1 . TRP   A 210 ? 0.244 0.115 0.442 -0.031 -0.045 -0.058 209 TRP   AAA CD1 
1627 C  CD2 . TRP   A 210 ? 0.245 0.026 0.382 -0.029 0.013  -0.041 209 TRP   AAA CD2 
1628 N  NE1 . TRP   A 210 ? 0.246 0.090 0.424 0.019  0.007  -0.043 209 TRP   AAA NE1 
1629 C  CE2 . TRP   A 210 ? 0.223 0.090 0.379 0.027  0.025  -0.045 209 TRP   AAA CE2 
1630 C  CE3 . TRP   A 210 ? 0.249 0.009 0.382 -0.007 -0.021 -0.029 209 TRP   AAA CE3 
1631 C  CZ2 . TRP   A 210 ? 0.273 0.050 0.399 -0.000 -0.008 -0.019 209 TRP   AAA CZ2 
1632 C  CZ3 . TRP   A 210 ? 0.263 0.011 0.392 -0.033 -0.019 -0.017 209 TRP   AAA CZ3 
1633 C  CH2 . TRP   A 210 ? 0.273 0.050 0.394 0.011  0.014  -0.013 209 TRP   AAA CH2 
1634 N  N   . ILE   A 211 ? 0.283 0.110 0.375 -0.026 -0.020 -0.057 210 ILE   AAA N   
1635 C  CA  . ILE   A 211 ? 0.319 0.016 0.382 0.039  -0.009 -0.041 210 ILE   AAA CA  
1636 C  C   . ILE   A 211 ? 0.319 0.043 0.326 0.020  -0.013 -0.021 210 ILE   AAA C   
1637 O  O   . ILE   A 211 ? 0.326 0.085 0.375 0.049  -0.023 -0.093 210 ILE   AAA O   
1638 C  CB  . ILE   A 211 ? 0.292 0.014 0.401 0.028  0.009  -0.043 210 ILE   AAA CB  
1639 C  CG1 . ILE   A 211 ? 0.296 0.020 0.438 0.010  -0.007 -0.003 210 ILE   AAA CG1 
1640 C  CG2 . ILE   A 211 ? 0.322 0.111 0.417 0.043  0.050  -0.061 210 ILE   AAA CG2 
1641 C  CD1 . ILE   A 211 ? 0.388 0.088 0.439 0.029  -0.024 -0.025 210 ILE   AAA CD1 
1642 N  N   . ILE   A 212 ? 0.328 0.102 0.373 -0.010 0.018  -0.073 211 ILE   AAA N   
1643 C  CA  . ILE   A 212 ? 0.333 0.020 0.376 0.018  0.030  -0.051 211 ILE   AAA CA  
1644 C  C   . ILE   A 212 ? 0.306 0.105 0.334 0.003  -0.023 -0.028 211 ILE   AAA C   
1645 O  O   . ILE   A 212 ? 0.340 0.065 0.345 -0.015 -0.004 -0.044 211 ILE   AAA O   
1646 C  CB  . ILE   A 212 ? 0.330 0.011 0.378 -0.003 0.007  -0.032 211 ILE   AAA CB  
1647 C  CG1 . ILE   A 212 ? 0.361 0.109 0.399 0.029  0.040  -0.023 211 ILE   AAA CG1 
1648 C  CG2 . ILE   A 212 ? 0.337 0.065 0.424 0.047  -0.044 -0.015 211 ILE   AAA CG2 
1649 C  CD1 . ILE   A 212 ? 0.324 0.090 0.427 0.016  0.047  -0.054 211 ILE   AAA CD1 
1650 N  N   . CYS   A 213 ? 0.347 0.016 0.409 0.039  -0.010 -0.049 212 CYS   AAA N   
1651 C  CA  . CYS   A 213 ? 0.304 0.158 0.375 -0.045 -0.009 -0.044 212 CYS   AAA CA  
1652 C  C   . CYS   A 213 ? 0.297 0.164 0.337 -0.031 -0.017 -0.015 212 CYS   AAA C   
1653 O  O   . CYS   A 213 ? 0.315 0.098 0.387 -0.006 -0.003 -0.043 212 CYS   AAA O   
1654 C  CB  . CYS   A 213 ? 0.326 0.014 0.426 -0.019 0.002  -0.014 212 CYS   AAA CB  
1655 S  SG  . CYS   A 213 ? 0.379 0.089 0.479 0.015  0.005  -0.063 212 CYS   AAA SG  
1656 N  N   . LYS   A 214 ? 0.338 0.107 0.339 -0.000 0.003  -0.004 213 LYS   AAA N   
1657 C  CA  . LYS   A 214 ? 0.381 0.115 0.359 -0.065 0.026  -0.085 213 LYS   AAA CA  
1658 C  C   . LYS   A 214 ? 0.333 0.060 0.380 -0.001 0.055  -0.049 213 LYS   AAA C   
1659 O  O   . LYS   A 214 ? 0.356 0.077 0.414 0.018  0.010  -0.056 213 LYS   AAA O   
1660 C  CB  . LYS   A 214 ? 0.439 0.200 0.397 -0.080 -0.017 -0.067 213 LYS   AAA CB  
1661 C  CG  . LYS   A 214 ? 0.521 0.364 0.440 0.026  -0.016 -0.061 213 LYS   AAA CG  
1662 C  CD  . LYS   A 214 ? 0.533 0.321 0.446 0.001  0.002  -0.060 213 LYS   AAA CD  
1663 C  CE  . LYS   A 214 ? 0.463 0.351 0.498 -0.006 0.051  0.006  213 LYS   AAA CE  
1664 N  NZ  . LYS   A 214 ? 0.671 0.294 0.561 0.058  0.005  0.024  213 LYS   AAA NZ  
1665 N  N   . GLU   A 215 ? 0.347 0.028 0.378 0.067  0.011  -0.033 214 GLU   AAA N   
1666 C  CA  . GLU   A 215 ? 0.349 0.019 0.400 0.056  -0.007 -0.038 214 GLU   AAA CA  
1667 C  C   . GLU   A 215 ? 0.272 0.041 0.390 -0.005 0.009  -0.039 214 GLU   AAA C   
1668 O  O   . GLU   A 215 ? 0.308 0.022 0.380 0.021  0.018  0.004  214 GLU   AAA O   
1669 C  CB  . GLU   A 215 ? 0.442 0.027 0.488 0.091  0.095  -0.010 214 GLU   AAA CB  
1670 C  CG  . GLU   A 215 ? 0.639 0.036 0.599 0.105  0.139  0.025  214 GLU   AAA CG  
1671 C  CD  . GLU   A 215 ? 0.448 0.048 0.648 0.013  0.178  -0.007 214 GLU   AAA CD  
1672 O  OE1 . GLU   A 215 ? 0.557 0.150 0.476 0.084  0.106  0.025  214 GLU   AAA OE1 
1673 O  OE2 . GLU   A 215 ? 0.615 0.346 0.691 0.055  0.143  0.037  214 GLU   AAA OE2 
1674 N  N   . SER   A 216 ? 0.286 0.024 0.415 0.022  -0.017 -0.047 215 SER   AAA N   
1675 C  CA  . SER   A 216 ? 0.257 0.108 0.414 0.037  -0.013 -0.092 215 SER   AAA CA  
1676 C  C   . SER   A 216 ? 0.300 0.081 0.343 0.021  0.003  -0.034 215 SER   AAA C   
1677 O  O   . SER   A 216 ? 0.350 0.149 0.353 0.012  -0.005 -0.012 215 SER   AAA O   
1678 C  CB  . SER   A 216 ? 0.268 0.076 0.387 0.032  0.005  -0.086 215 SER   AAA CB  
1679 O  OG  . SER   A 216 ? 0.306 0.074 0.410 0.016  0.020  -0.053 215 SER   AAA OG  
1680 N  N   . ILE   A 217 ? 0.306 0.053 0.362 0.016  -0.003 -0.019 216 ILE   AAA N   
1681 C  CA  . ILE   A 217 ? 0.273 0.197 0.346 -0.018 -0.006 -0.053 216 ILE   AAA CA  
1682 C  C   . ILE   A 217 ? 0.242 0.177 0.422 -0.057 -0.002 -0.017 216 ILE   AAA C   
1683 O  O   . ILE   A 217 ? 0.335 0.147 0.408 -0.026 0.010  -0.041 216 ILE   AAA O   
1684 C  CB  . ILE   A 217 ? 0.276 0.164 0.338 -0.043 0.005  -0.061 216 ILE   AAA CB  
1685 C  CG1 . ILE   A 217 ? 0.306 0.111 0.366 -0.030 0.028  -0.057 216 ILE   AAA CG1 
1686 C  CG2 . ILE   A 217 ? 0.298 0.151 0.347 -0.039 -0.008 -0.042 216 ILE   AAA CG2 
1687 C  CD1 . ILE   A 217 ? 0.357 0.106 0.321 -0.052 0.045  -0.023 216 ILE   AAA CD1 
1688 N  N   . SER   A 218 ? 0.304 0.014 0.403 -0.047 0.016  -0.014 217 SER   AAA N   
1689 C  CA  A SER   A 218 ? 0.302 0.055 0.416 -0.035 0.015  -0.019 217 SER   AAA CA  
1690 C  CA  B SER   A 218 ? 0.300 0.093 0.415 -0.019 0.023  -0.029 217 SER   AAA CA  
1691 C  C   . SER   A 218 ? 0.230 0.115 0.412 -0.010 0.014  -0.003 217 SER   AAA C   
1692 O  O   . SER   A 218 ? 0.281 0.118 0.414 -0.000 0.006  -0.024 217 SER   AAA O   
1693 C  CB  A SER   A 218 ? 0.331 0.030 0.443 -0.059 0.013  -0.018 217 SER   AAA CB  
1694 C  CB  B SER   A 218 ? 0.293 0.191 0.444 -0.044 0.050  -0.039 217 SER   AAA CB  
1695 O  OG  A SER   A 218 ? 0.369 0.030 0.417 -0.067 0.022  -0.021 217 SER   AAA OG  
1696 O  OG  B SER   A 218 ? 0.299 0.224 0.389 -0.022 0.044  -0.027 217 SER   AAA OG  
1697 N  N   . VAL   A 219 ? 0.282 0.067 0.418 0.025  0.003  -0.016 218 VAL   AAA N   
1698 C  CA  . VAL   A 219 ? 0.326 0.034 0.374 0.035  0.024  -0.054 218 VAL   AAA CA  
1699 C  C   . VAL   A 219 ? 0.288 0.270 0.310 0.016  0.021  -0.092 218 VAL   AAA C   
1700 O  O   . VAL   A 219 ? 0.332 0.139 0.420 0.038  0.018  -0.075 218 VAL   AAA O   
1701 C  CB  . VAL   A 219 ? 0.302 0.127 0.388 0.057  0.040  -0.038 218 VAL   AAA CB  
1702 C  CG1 . VAL   A 219 ? 0.344 0.119 0.391 0.058  0.004  -0.015 218 VAL   AAA CG1 
1703 C  CG2 . VAL   A 219 ? 0.291 0.180 0.411 0.034  0.016  -0.046 218 VAL   AAA CG2 
1704 N  N   . SER   A 220 ? 0.292 0.159 0.394 -0.020 -0.026 -0.047 219 SER   AAA N   
1705 C  CA  . SER   A 220 ? 0.279 0.242 0.406 -0.026 -0.005 -0.021 219 SER   AAA CA  
1706 C  C   . SER   A 220 ? 0.249 0.078 0.411 0.014  -0.002 -0.083 219 SER   AAA C   
1707 O  O   . SER   A 220 ? 0.275 0.058 0.456 0.024  0.015  -0.061 219 SER   AAA O   
1708 C  CB  . SER   A 220 ? 0.286 0.184 0.442 0.008  -0.026 -0.051 219 SER   AAA CB  
1709 O  OG  . SER   A 220 ? 0.340 0.102 0.450 -0.018 -0.002 -0.045 219 SER   AAA OG  
1710 N  N   . SER   A 221 ? 0.283 0.283 0.393 0.115  0.015  -0.063 220 SER   AAA N   
1711 C  CA  A SER   A 221 ? 0.317 0.246 0.390 0.059  0.032  -0.044 220 SER   AAA CA  
1712 C  CA  B SER   A 221 ? 0.337 0.268 0.390 0.055  0.029  -0.043 220 SER   AAA CA  
1713 C  C   . SER   A 221 ? 0.250 0.188 0.401 0.015  0.048  -0.060 220 SER   AAA C   
1714 O  O   . SER   A 221 ? 0.346 0.199 0.373 0.056  0.028  -0.026 220 SER   AAA O   
1715 C  CB  A SER   A 221 ? 0.327 0.231 0.379 0.051  0.056  -0.032 220 SER   AAA CB  
1716 C  CB  B SER   A 221 ? 0.354 0.286 0.444 0.059  0.062  -0.030 220 SER   AAA CB  
1717 O  OG  A SER   A 221 ? 0.317 0.122 0.396 0.067  0.049  -0.040 220 SER   AAA OG  
1718 O  OG  B SER   A 221 ? 0.394 0.234 0.541 0.046  0.016  -0.056 220 SER   AAA OG  
1719 N  N   . GLU   A 222 ? 0.298 0.224 0.456 0.003  0.005  -0.063 221 GLU   AAA N   
1720 C  CA  . GLU   A 222 ? 0.262 0.259 0.410 0.015  -0.016 -0.029 221 GLU   AAA CA  
1721 C  C   . GLU   A 222 ? 0.274 0.260 0.396 0.027  -0.035 -0.071 221 GLU   AAA C   
1722 O  O   . GLU   A 222 ? 0.309 0.277 0.424 0.059  -0.001 -0.092 221 GLU   AAA O   
1723 C  CB  . GLU   A 222 ? 0.280 0.304 0.386 -0.006 0.015  -0.046 221 GLU   AAA CB  
1724 C  CG  . GLU   A 222 ? 0.281 0.128 0.487 -0.007 0.015  0.006  221 GLU   AAA CG  
1725 C  CD  . GLU   A 222 ? 0.293 0.278 0.451 -0.037 0.014  0.032  221 GLU   AAA CD  
1726 O  OE1 . GLU   A 222 ? 0.308 0.303 0.439 0.057  -0.006 -0.007 221 GLU   AAA OE1 
1727 O  OE2 . GLU   A 222 ? 0.370 0.462 0.531 0.086  0.049  -0.068 221 GLU   AAA OE2 
1728 N  N   . GLN   A 223 ? 0.304 0.240 0.381 0.024  -0.010 -0.069 222 GLN   AAA N   
1729 C  CA  . GLN   A 223 ? 0.295 0.143 0.406 -0.010 0.028  -0.040 222 GLN   AAA CA  
1730 C  C   . GLN   A 223 ? 0.288 0.171 0.392 -0.015 0.009  -0.018 222 GLN   AAA C   
1731 O  O   . GLN   A 223 ? 0.306 0.128 0.424 0.018  0.017  -0.055 222 GLN   AAA O   
1732 C  CB  . GLN   A 223 ? 0.363 0.172 0.385 -0.076 -0.023 -0.055 222 GLN   AAA CB  
1733 C  CG  . GLN   A 223 ? 0.296 0.123 0.481 -0.007 -0.052 -0.056 222 GLN   AAA CG  
1734 C  CD  . GLN   A 223 ? 0.313 0.151 0.418 -0.039 -0.033 -0.040 222 GLN   AAA CD  
1735 O  OE1 . GLN   A 223 ? 0.317 0.087 0.414 -0.003 0.003  -0.011 222 GLN   AAA OE1 
1736 N  NE2 . GLN   A 223 ? 0.378 0.181 0.494 -0.006 0.028  -0.112 222 GLN   AAA NE2 
1737 N  N   . LEU   A 224 ? 0.332 0.196 0.412 0.073  0.011  -0.017 223 LEU   AAA N   
1738 C  CA  . LEU   A 224 ? 0.307 0.210 0.416 0.002  -0.014 -0.055 223 LEU   AAA CA  
1739 C  C   . LEU   A 224 ? 0.255 0.268 0.408 0.046  0.002  -0.073 223 LEU   AAA C   
1740 O  O   . LEU   A 224 ? 0.264 0.157 0.472 0.004  -0.005 -0.070 223 LEU   AAA O   
1741 C  CB  . LEU   A 224 ? 0.320 0.291 0.378 0.043  0.014  -0.062 223 LEU   AAA CB  
1742 C  CG  . LEU   A 224 ? 0.324 0.234 0.372 0.026  -0.002 -0.020 223 LEU   AAA CG  
1743 C  CD1 . LEU   A 224 ? 0.404 0.259 0.445 0.037  0.042  -0.046 223 LEU   AAA CD1 
1744 C  CD2 . LEU   A 224 ? 0.305 0.341 0.386 0.004  -0.045 0.026  223 LEU   AAA CD2 
1745 N  N   . ALA   A 225 ? 0.264 0.260 0.391 0.023  -0.015 -0.066 224 ALA   AAA N   
1746 C  CA  . ALA   A 225 ? 0.272 0.290 0.375 0.039  -0.029 -0.071 224 ALA   AAA CA  
1747 C  C   . ALA   A 225 ? 0.308 0.200 0.348 0.023  -0.027 -0.049 224 ALA   AAA C   
1748 O  O   . ALA   A 225 ? 0.327 0.189 0.368 -0.000 0.015  -0.068 224 ALA   AAA O   
1749 C  CB  . ALA   A 225 ? 0.282 0.311 0.439 0.019  -0.008 -0.051 224 ALA   AAA CB  
1750 N  N   . GLN   A 226 ? 0.293 0.225 0.367 -0.016 0.005  -0.009 225 GLN   AAA N   
1751 C  CA  . GLN   A 226 ? 0.319 0.145 0.388 -0.007 0.022  -0.006 225 GLN   AAA CA  
1752 C  C   . GLN   A 226 ? 0.293 0.113 0.345 0.009  -0.017 -0.014 225 GLN   AAA C   
1753 O  O   . GLN   A 226 ? 0.364 0.150 0.391 0.001  0.019  0.005  225 GLN   AAA O   
1754 C  CB  . GLN   A 226 ? 0.257 0.162 0.394 0.035  0.028  0.009  225 GLN   AAA CB  
1755 C  CG  . GLN   A 226 ? 0.303 0.122 0.462 0.010  0.014  -0.027 225 GLN   AAA CG  
1756 C  CD  . GLN   A 226 ? 0.320 0.173 0.452 0.034  -0.016 0.032  225 GLN   AAA CD  
1757 O  OE1 . GLN   A 226 ? 0.395 0.101 0.473 -0.014 -0.016 0.011  225 GLN   AAA OE1 
1758 N  NE2 . GLN   A 226 ? 0.413 0.020 0.520 -0.039 -0.007 -0.009 225 GLN   AAA NE2 
1759 N  N   . PHE   A 227 ? 0.253 0.123 0.358 0.015  -0.005 -0.019 226 PHE   AAA N   
1760 C  CA  . PHE   A 227 ? 0.262 0.112 0.367 0.029  0.004  -0.006 226 PHE   AAA CA  
1761 C  C   . PHE   A 227 ? 0.320 0.046 0.376 0.017  0.017  -0.027 226 PHE   AAA C   
1762 O  O   . PHE   A 227 ? 0.332 0.115 0.386 0.039  0.014  -0.028 226 PHE   AAA O   
1763 C  CB  . PHE   A 227 ? 0.308 0.082 0.396 -0.038 0.014  -0.040 226 PHE   AAA CB  
1764 C  CG  . PHE   A 227 ? 0.322 0.188 0.382 0.016  -0.004 -0.024 226 PHE   AAA CG  
1765 C  CD1 . PHE   A 227 ? 0.443 0.205 0.403 0.062  0.034  -0.023 226 PHE   AAA CD1 
1766 C  CD2 . PHE   A 227 ? 0.352 0.211 0.391 -0.059 -0.019 -0.023 226 PHE   AAA CD2 
1767 C  CE1 . PHE   A 227 ? 0.457 0.293 0.411 0.083  0.049  0.022  226 PHE   AAA CE1 
1768 C  CE2 . PHE   A 227 ? 0.423 0.251 0.357 -0.032 -0.021 -0.032 226 PHE   AAA CE2 
1769 C  CZ  . PHE   A 227 ? 0.343 0.289 0.410 0.123  0.018  0.019  226 PHE   AAA CZ  
1770 N  N   . ARG   A 228 ? 0.320 0.126 0.375 0.051  0.002  -0.012 227 ARG   AAA N   
1771 C  CA  . ARG   A 228 ? 0.372 0.059 0.390 0.019  0.000  -0.041 227 ARG   AAA CA  
1772 C  C   . ARG   A 228 ? 0.333 0.099 0.395 -0.023 -0.009 -0.003 227 ARG   AAA C   
1773 O  O   . ARG   A 228 ? 0.377 0.132 0.427 0.025  0.021  0.027  227 ARG   AAA O   
1774 C  CB  . ARG   A 228 ? 0.343 0.189 0.404 0.029  0.000  -0.081 227 ARG   AAA CB  
1775 C  CG  . ARG   A 228 ? 0.336 0.262 0.388 0.038  0.016  -0.088 227 ARG   AAA CG  
1776 C  CD  . ARG   A 228 ? 0.454 0.224 0.511 0.077  -0.070 -0.125 227 ARG   AAA CD  
1777 N  NE  . ARG   A 228 ? 0.436 0.249 0.492 0.089  -0.089 -0.095 227 ARG   AAA NE  
1778 C  CZ  . ARG   A 228 ? 0.474 0.200 0.481 0.104  -0.076 -0.037 227 ARG   AAA CZ  
1779 N  NH1 . ARG   A 228 ? 0.550 0.376 0.488 0.169  -0.099 -0.099 227 ARG   AAA NH1 
1780 N  NH2 . ARG   A 228 ? 0.540 0.279 0.554 0.102  -0.142 -0.044 227 ARG   AAA NH2 
1781 N  N   . SER   A 229 ? 0.291 0.104 0.405 -0.028 0.007  -0.004 228 SER   AAA N   
1782 C  CA  . SER   A 229 ? 0.305 0.106 0.411 -0.009 -0.011 0.025  228 SER   AAA CA  
1783 C  C   . SER   A 229 ? 0.285 0.161 0.409 0.003  -0.021 0.018  228 SER   AAA C   
1784 O  O   . SER   A 229 ? 0.313 0.156 0.422 0.060  -0.041 0.006  228 SER   AAA O   
1785 C  CB  . SER   A 229 ? 0.394 0.257 0.467 -0.107 0.002  0.071  228 SER   AAA CB  
1786 O  OG  . SER   A 229 ? 0.556 0.257 0.561 -0.065 -0.048 -0.006 228 SER   AAA OG  
1787 N  N   . LEU   A 230 ? 0.300 0.154 0.388 -0.006 -0.016 0.033  229 LEU   AAA N   
1788 C  CA  . LEU   A 230 ? 0.312 0.122 0.423 -0.008 -0.010 0.029  229 LEU   AAA CA  
1789 C  C   . LEU   A 230 ? 0.305 0.138 0.340 0.021  0.032  0.019  229 LEU   AAA C   
1790 O  O   . LEU   A 230 ? 0.400 0.180 0.423 0.037  0.025  -0.053 229 LEU   AAA O   
1791 C  CB  . LEU   A 230 ? 0.336 0.131 0.411 0.037  -0.035 -0.038 229 LEU   AAA CB  
1792 C  CG  . LEU   A 230 ? 0.514 0.132 0.532 0.016  -0.104 -0.030 229 LEU   AAA CG  
1793 C  CD1 . LEU   A 230 ? 0.485 0.030 0.694 -0.010 -0.116 -0.123 229 LEU   AAA CD1 
1794 C  CD2 . LEU   A 230 ? 0.427 0.145 0.517 0.049  -0.053 -0.049 229 LEU   AAA CD2 
1795 N  N   . LEU   A 231 ? 0.286 0.153 0.343 0.070  0.013  0.013  230 LEU   AAA N   
1796 C  CA  . LEU   A 231 ? 0.305 0.063 0.379 0.046  0.014  -0.004 230 LEU   AAA CA  
1797 C  C   . LEU   A 231 ? 0.300 0.052 0.388 0.008  0.002  -0.022 230 LEU   AAA C   
1798 O  O   . LEU   A 231 ? 0.293 0.078 0.457 0.013  0.007  -0.022 230 LEU   AAA O   
1799 C  CB  . LEU   A 231 ? 0.324 0.173 0.401 0.090  -0.008 -0.023 230 LEU   AAA CB  
1800 C  CG  . LEU   A 231 ? 0.320 0.169 0.456 0.083  -0.052 -0.011 230 LEU   AAA CG  
1801 C  CD1 . LEU   A 231 ? 0.368 0.277 0.439 0.093  -0.078 -0.021 230 LEU   AAA CD1 
1802 C  CD2 . LEU   A 231 ? 0.332 0.200 0.456 0.071  -0.023 -0.064 230 LEU   AAA CD2 
1803 N  N   . SER   A 232 ? 0.375 0.056 0.427 -0.019 0.008  -0.016 231 SER   AAA N   
1804 C  CA  . SER   A 232 ? 0.367 0.017 0.436 -0.000 -0.027 0.006  231 SER   AAA CA  
1805 C  C   . SER   A 232 ? 0.338 0.030 0.460 0.042  -0.021 -0.071 231 SER   AAA C   
1806 O  O   . SER   A 232 ? 0.358 0.047 0.494 0.006  0.022  -0.051 231 SER   AAA O   
1807 C  CB  . SER   A 232 ? 0.388 0.043 0.562 0.031  0.016  -0.091 231 SER   AAA CB  
1808 O  OG  . SER   A 232 ? 0.436 0.134 0.500 0.069  0.021  -0.033 231 SER   AAA OG  
1809 N  N   . ASN   A 233 ? 0.349 0.059 0.398 0.049  -0.030 -0.043 232 ASN   AAA N   
1810 C  CA  . ASN   A 233 ? 0.300 0.072 0.404 0.035  0.014  -0.083 232 ASN   AAA CA  
1811 C  C   . ASN   A 233 ? 0.305 0.047 0.359 0.026  0.024  -0.048 232 ASN   AAA C   
1812 O  O   . ASN   A 233 ? 0.325 0.169 0.440 -0.046 0.033  0.032  232 ASN   AAA O   
1813 C  CB  . ASN   A 233 ? 0.326 0.182 0.426 0.034  0.007  0.046  232 ASN   AAA CB  
1814 C  CG  . ASN   A 233 ? 0.326 0.238 0.370 0.015  0.019  0.025  232 ASN   AAA CG  
1815 O  OD1 . ASN   A 233 ? 0.384 0.260 0.418 0.059  -0.017 -0.012 232 ASN   AAA OD1 
1816 N  ND2 . ASN   A 233 ? 0.305 0.033 0.380 0.024  0.034  0.006  232 ASN   AAA ND2 
1817 N  N   . VAL   A 234 ? 0.333 0.117 0.406 0.006  0.046  -0.042 233 VAL   AAA N   
1818 C  CA  . VAL   A 234 ? 0.311 0.176 0.420 0.037  -0.013 -0.087 233 VAL   AAA CA  
1819 C  C   . VAL   A 234 ? 0.290 0.051 0.384 0.013  0.016  -0.066 233 VAL   AAA C   
1820 O  O   . VAL   A 234 ? 0.349 0.156 0.443 0.071  0.025  0.005  233 VAL   AAA O   
1821 C  CB  . VAL   A 234 ? 0.353 0.263 0.426 0.079  0.013  -0.049 233 VAL   AAA CB  
1822 C  CG1 . VAL   A 234 ? 0.389 0.290 0.471 0.037  -0.008 -0.023 233 VAL   AAA CG1 
1823 C  CG2 . VAL   A 234 ? 0.390 0.346 0.494 0.056  0.021  0.049  233 VAL   AAA CG2 
1824 N  N   . GLU   A 235 ? 0.361 0.028 0.412 0.022  -0.001 -0.024 234 GLU   AAA N   
1825 C  CA  . GLU   A 235 ? 0.335 0.096 0.450 0.037  -0.017 -0.032 234 GLU   AAA CA  
1826 C  C   . GLU   A 235 ? 0.368 0.123 0.453 0.033  0.001  -0.020 234 GLU   AAA C   
1827 O  O   . GLU   A 235 ? 0.407 0.036 0.460 0.027  0.011  0.009  234 GLU   AAA O   
1828 C  CB  . GLU   A 235 ? 0.370 0.098 0.478 0.053  -0.004 -0.037 234 GLU   AAA CB  
1829 C  CG  . GLU   A 235 ? 0.356 0.167 0.457 0.010  0.023  -0.035 234 GLU   AAA CG  
1830 C  CD  . GLU   A 235 ? 0.475 0.171 0.514 0.071  -0.022 -0.048 234 GLU   AAA CD  
1831 O  OE1 . GLU   A 235 ? 0.504 0.095 0.552 0.046  -0.028 -0.059 234 GLU   AAA OE1 
1832 O  OE2 . GLU   A 235 ? 0.749 0.198 0.570 0.017  -0.014 -0.108 234 GLU   AAA OE2 
1833 N  N   . GLY   A 236 ? 0.336 0.166 0.460 0.017  0.006  0.043  235 GLY   AAA N   
1834 C  CA  . GLY   A 236 ? 0.357 0.132 0.439 0.101  0.017  -0.008 235 GLY   AAA CA  
1835 C  C   . GLY   A 236 ? 0.531 0.127 0.461 0.069  -0.022 0.019  235 GLY   AAA C   
1836 O  O   . GLY   A 236 ? 0.554 0.306 0.556 0.106  -0.062 0.074  235 GLY   AAA O   
1837 N  N   . ASP   A 237 ? 0.474 0.091 0.436 0.093  -0.012 0.101  236 ASP   AAA N   
1838 C  CA  . ASP   A 237 ? 0.531 0.100 0.457 0.137  -0.033 0.081  236 ASP   AAA CA  
1839 C  C   . ASP   A 237 ? 0.545 0.128 0.500 0.160  -0.034 0.030  236 ASP   AAA C   
1840 O  O   . ASP   A 237 ? 0.585 0.233 0.464 0.091  0.024  0.027  236 ASP   AAA O   
1841 C  CB  . ASP   A 237 ? 0.516 0.112 0.489 0.066  -0.003 0.089  236 ASP   AAA CB  
1842 C  CG  . ASP   A 237 ? 0.531 0.211 0.472 0.026  0.001  0.076  236 ASP   AAA CG  
1843 O  OD1 . ASP   A 237 ? 0.664 0.265 0.506 -0.037 0.046  0.008  236 ASP   AAA OD1 
1844 O  OD2 . ASP   A 237 ? 0.571 0.301 0.529 -0.022 -0.013 0.031  236 ASP   AAA OD2 
1845 N  N   . ASN   A 238 ? 0.558 0.092 0.491 0.116  -0.012 0.029  237 ASN   AAA N   
1846 C  CA  A ASN   A 238 ? 0.586 0.127 0.484 0.219  -0.041 -0.034 237 ASN   AAA CA  
1847 C  CA  B ASN   A 238 ? 0.596 0.277 0.443 0.116  -0.018 0.019  237 ASN   AAA CA  
1848 C  C   . ASN   A 238 ? 0.478 0.208 0.474 0.170  0.001  0.056  237 ASN   AAA C   
1849 O  O   . ASN   A 238 ? 0.446 0.184 0.472 0.139  0.038  0.059  237 ASN   AAA O   
1850 C  CB  A ASN   A 238 ? 0.691 0.049 0.567 0.121  -0.032 -0.116 237 ASN   AAA CB  
1851 C  CB  B ASN   A 238 ? 0.610 0.283 0.417 0.160  -0.077 0.108  237 ASN   AAA CB  
1852 C  CG  A ASN   A 238 ? 0.589 0.154 0.533 0.108  -0.140 -0.070 237 ASN   AAA CG  
1853 C  CG  B ASN   A 238 ? 0.678 0.311 0.378 0.038  -0.101 0.095  237 ASN   AAA CG  
1854 O  OD1 A ASN   A 238 ? 0.395 0.227 0.608 -0.095 -0.114 -0.054 237 ASN   AAA OD1 
1855 O  OD1 B ASN   A 238 ? 0.865 0.216 0.528 -0.014 -0.141 0.061  237 ASN   AAA OD1 
1856 N  ND2 A ASN   A 238 ? 0.602 0.277 0.573 0.189  -0.076 0.080  237 ASN   AAA ND2 
1857 N  ND2 B ASN   A 238 ? 0.696 0.146 0.461 0.145  -0.077 0.014  237 ASN   AAA ND2 
1858 N  N   . ALA   A 239 ? 0.532 0.355 0.438 0.135  0.040  0.013  238 ALA   AAA N   
1859 C  CA  . ALA   A 239 ? 0.460 0.388 0.403 0.085  0.027  -0.014 238 ALA   AAA CA  
1860 C  C   . ALA   A 239 ? 0.441 0.293 0.415 0.226  -0.014 -0.004 238 ALA   AAA C   
1861 O  O   . ALA   A 239 ? 0.526 0.308 0.539 0.266  0.011  0.055  238 ALA   AAA O   
1862 C  CB  . ALA   A 239 ? 0.484 0.543 0.417 0.035  0.058  0.080  238 ALA   AAA CB  
1863 N  N   . VAL   A 240 ? 0.404 0.136 0.477 0.078  -0.022 -0.025 239 VAL   AAA N   
1864 C  CA  . VAL   A 240 ? 0.401 0.221 0.424 0.136  0.002  -0.039 239 VAL   AAA CA  
1865 C  C   . VAL   A 240 ? 0.373 0.203 0.437 0.116  0.042  0.001  239 VAL   AAA C   
1866 O  O   . VAL   A 240 ? 0.439 0.163 0.455 0.155  0.015  -0.005 239 VAL   AAA O   
1867 C  CB  . VAL   A 240 ? 0.441 0.180 0.491 0.102  -0.032 -0.029 239 VAL   AAA CB  
1868 C  CG1 . VAL   A 240 ? 0.528 0.253 0.419 0.058  -0.020 -0.034 239 VAL   AAA CG1 
1869 C  CG2 . VAL   A 240 ? 0.565 0.140 0.460 -0.002 -0.007 -0.035 239 VAL   AAA CG2 
1870 N  N   . PRO   A 241 ? 0.402 0.205 0.418 0.108  0.029  0.013  240 PRO   AAA N   
1871 C  CA  . PRO   A 241 ? 0.424 0.019 0.431 0.055  0.013  0.002  240 PRO   AAA CA  
1872 C  C   . PRO   A 241 ? 0.438 0.176 0.397 0.078  -0.016 0.033  240 PRO   AAA C   
1873 O  O   . PRO   A 241 ? 0.474 0.186 0.445 0.045  0.035  -0.021 240 PRO   AAA O   
1874 C  CB  . PRO   A 241 ? 0.459 0.314 0.432 0.081  0.057  0.075  240 PRO   AAA CB  
1875 C  CG  . PRO   A 241 ? 0.475 0.428 0.446 0.084  0.042  0.034  240 PRO   AAA CG  
1876 C  CD  . PRO   A 241 ? 0.426 0.353 0.426 0.164  0.056  0.034  240 PRO   AAA CD  
1877 N  N   . MET   A 242 ? 0.436 0.012 0.469 0.011  0.000  0.015  241 MET   AAA N   
1878 C  CA  . MET   A 242 ? 0.435 0.049 0.470 0.033  -0.017 -0.045 241 MET   AAA CA  
1879 C  C   . MET   A 242 ? 0.431 0.039 0.456 0.057  0.016  0.019  241 MET   AAA C   
1880 O  O   . MET   A 242 ? 0.421 0.254 0.416 -0.109 -0.042 0.052  241 MET   AAA O   
1881 C  CB  . MET   A 242 ? 0.417 0.192 0.549 0.130  0.005  0.021  241 MET   AAA CB  
1882 C  CG  . MET   A 242 ? 0.541 0.169 0.622 0.168  0.114  -0.001 241 MET   AAA CG  
1883 S  SD  . MET   A 242 ? 0.401 0.142 0.541 0.064  0.023  -0.048 241 MET   AAA SD  
1884 C  CE  . MET   A 242 ? 0.389 0.024 0.527 -0.040 0.032  -0.032 241 MET   AAA CE  
1885 N  N   . GLN   A 243 ? 0.400 0.018 0.463 -0.033 -0.013 0.063  242 GLN   AAA N   
1886 C  CA  . GLN   A 243 ? 0.430 0.067 0.475 0.018  -0.022 0.043  242 GLN   AAA CA  
1887 C  C   . GLN   A 243 ? 0.373 0.089 0.395 0.046  0.027  0.065  242 GLN   AAA C   
1888 O  O   . GLN   A 243 ? 0.340 0.154 0.430 -0.014 0.041  0.021  242 GLN   AAA O   
1889 C  CB  . GLN   A 243 ? 0.621 0.101 0.554 0.080  -0.054 0.090  242 GLN   AAA CB  
1890 C  CG  . GLN   A 243 ? 0.846 0.058 0.672 0.087  -0.154 -0.017 242 GLN   AAA CG  
1891 C  CD  . GLN   A 243 ? 0.651 0.154 0.650 0.306  -0.044 -0.023 242 GLN   AAA CD  
1892 O  OE1 . GLN   A 243 ? 0.832 0.248 0.632 0.078  0.102  -0.041 242 GLN   AAA OE1 
1893 N  NE2 . GLN   A 243 ? 0.850 0.455 0.737 0.238  -0.019 0.167  242 GLN   AAA NE2 
1894 N  N   . HIS   A 244 ? 0.327 0.255 0.420 0.049  -0.009 -0.045 243 HIS   AAA N   
1895 C  CA  . HIS   A 244 ? 0.332 0.162 0.398 0.094  0.002  -0.009 243 HIS   AAA CA  
1896 C  C   . HIS   A 244 ? 0.329 0.136 0.379 0.014  0.006  -0.061 243 HIS   AAA C   
1897 O  O   . HIS   A 244 ? 0.352 0.032 0.408 0.018  0.014  -0.017 243 HIS   AAA O   
1898 C  CB  . HIS   A 244 ? 0.446 0.180 0.445 0.157  0.058  -0.011 243 HIS   AAA CB  
1899 C  CG  . HIS   A 244 ? 0.521 0.287 0.455 0.080  0.120  0.004  243 HIS   AAA CG  
1900 N  ND1 . HIS   A 244 ? 0.450 0.386 0.591 0.140  0.128  0.049  243 HIS   AAA ND1 
1901 C  CD2 . HIS   A 244 ? 0.636 0.218 0.498 -0.025 0.066  0.107  243 HIS   AAA CD2 
1902 C  CE1 . HIS   A 244 ? 0.688 0.100 0.662 0.035  0.116  -0.038 243 HIS   AAA CE1 
1903 N  NE2 . HIS   A 244 ? 0.741 0.041 0.620 0.044  0.064  0.093  243 HIS   AAA NE2 
1904 N  N   . ASN   A 245 ? 0.323 0.038 0.414 0.015  -0.015 -0.059 244 ASN   AAA N   
1905 C  CA  . ASN   A 245 ? 0.324 0.024 0.402 0.075  -0.016 -0.004 244 ASN   AAA CA  
1906 C  C   . ASN   A 245 ? 0.315 0.078 0.375 0.029  0.011  -0.039 244 ASN   AAA C   
1907 O  O   . ASN   A 245 ? 0.392 0.008 0.478 0.025  0.051  -0.005 244 ASN   AAA O   
1908 C  CB  . ASN   A 245 ? 0.341 0.041 0.409 0.066  -0.009 -0.039 244 ASN   AAA CB  
1909 C  CG  . ASN   A 245 ? 0.349 0.041 0.347 0.055  0.019  -0.077 244 ASN   AAA CG  
1910 O  OD1 . ASN   A 245 ? 0.345 0.013 0.370 0.034  0.022  -0.019 244 ASN   AAA OD1 
1911 N  ND2 . ASN   A 245 ? 0.402 0.031 0.355 0.092  0.018  -0.027 244 ASN   AAA ND2 
1912 N  N   . ASN   A 246 ? 0.299 0.013 0.406 0.043  0.021  0.004  245 ASN   AAA N   
1913 C  CA  . ASN   A 246 ? 0.329 0.019 0.454 0.064  -0.024 -0.021 245 ASN   AAA CA  
1914 C  C   . ASN   A 246 ? 0.277 0.013 0.456 -0.003 -0.001 0.014  245 ASN   AAA C   
1915 O  O   . ASN   A 246 ? 0.420 0.048 0.504 0.082  -0.025 -0.014 245 ASN   AAA O   
1916 C  CB  . ASN   A 246 ? 0.334 0.011 0.500 0.020  0.027  -0.040 245 ASN   AAA CB  
1917 C  CG  . ASN   A 246 ? 0.390 0.020 0.467 0.070  -0.022 -0.027 245 ASN   AAA CG  
1918 O  OD1 . ASN   A 246 ? 0.474 0.150 0.521 0.067  0.045  -0.010 245 ASN   AAA OD1 
1919 N  ND2 . ASN   A 246 ? 0.367 0.028 0.382 0.067  0.011  -0.056 245 ASN   AAA ND2 
1920 N  N   . ARG   A 247 ? 0.270 0.011 0.445 -0.023 0.015  -0.023 246 ARG   AAA N   
1921 C  CA  . ARG   A 247 ? 0.328 0.010 0.453 -0.031 0.071  -0.024 246 ARG   AAA CA  
1922 C  C   . ARG   A 247 ? 0.349 0.018 0.478 -0.012 0.058  -0.075 246 ARG   AAA C   
1923 O  O   . ARG   A 247 ? 0.339 0.099 0.462 0.039  0.036  -0.041 246 ARG   AAA O   
1924 C  CB  . ARG   A 247 ? 0.310 0.015 0.438 -0.032 0.046  -0.051 246 ARG   AAA CB  
1925 C  CG  . ARG   A 247 ? 0.355 0.009 0.462 -0.008 0.048  -0.036 246 ARG   AAA CG  
1926 C  CD  . ARG   A 247 ? 0.318 0.031 0.496 -0.044 0.061  -0.046 246 ARG   AAA CD  
1927 N  NE  . ARG   A 247 ? 0.335 0.021 0.470 -0.052 0.067  -0.059 246 ARG   AAA NE  
1928 C  CZ  . ARG   A 247 ? 0.338 0.076 0.446 -0.040 0.073  -0.057 246 ARG   AAA CZ  
1929 N  NH1 . ARG   A 247 ? 0.373 0.034 0.498 -0.100 0.042  -0.030 246 ARG   AAA NH1 
1930 N  NH2 . ARG   A 247 ? 0.383 0.064 0.540 -0.029 0.088  -0.013 246 ARG   AAA NH2 
1931 N  N   . PRO   A 248 ? 0.429 0.007 0.441 0.016  0.032  -0.001 247 PRO   AAA N   
1932 C  CA  . PRO   A 248 ? 0.488 0.039 0.463 -0.125 0.036  -0.020 247 PRO   AAA CA  
1933 C  C   . PRO   A 248 ? 0.453 0.024 0.457 -0.089 0.053  -0.017 247 PRO   AAA C   
1934 O  O   . PRO   A 248 ? 0.510 0.012 0.569 -0.016 0.032  -0.054 247 PRO   AAA O   
1935 C  CB  . PRO   A 248 ? 0.463 0.023 0.448 -0.036 0.084  -0.024 247 PRO   AAA CB  
1936 C  CG  . PRO   A 248 ? 0.561 0.155 0.480 0.006  0.091  -0.066 247 PRO   AAA CG  
1937 C  CD  . PRO   A 248 ? 0.475 0.153 0.370 0.056  0.069  -0.015 247 PRO   AAA CD  
1938 N  N   . THR   A 249 ? 0.358 0.065 0.465 -0.032 0.090  -0.049 248 THR   AAA N   
1939 C  CA  . THR   A 249 ? 0.359 0.020 0.530 -0.029 0.096  -0.083 248 THR   AAA CA  
1940 C  C   . THR   A 249 ? 0.356 0.028 0.519 -0.081 0.026  0.033  248 THR   AAA C   
1941 O  O   . THR   A 249 ? 0.420 0.017 0.511 0.014  0.050  -0.030 248 THR   AAA O   
1942 C  CB  . THR   A 249 ? 0.436 0.007 0.534 -0.021 0.080  -0.008 248 THR   AAA CB  
1943 O  OG1 . THR   A 249 ? 0.371 0.028 0.514 0.043  0.065  -0.082 248 THR   AAA OG1 
1944 C  CG2 . THR   A 249 ? 0.381 0.031 0.506 -0.072 0.038  -0.079 248 THR   AAA CG2 
1945 N  N   . GLN   A 250 ? 0.327 0.059 0.481 -0.013 0.066  -0.069 249 GLN   AAA N   
1946 C  CA  . GLN   A 250 ? 0.366 0.024 0.468 -0.026 0.058  -0.065 249 GLN   AAA CA  
1947 C  C   . GLN   A 250 ? 0.413 0.082 0.463 -0.016 0.043  -0.030 249 GLN   AAA C   
1948 O  O   . GLN   A 250 ? 0.419 0.146 0.444 -0.009 0.034  -0.051 249 GLN   AAA O   
1949 C  CB  . GLN   A 250 ? 0.367 0.055 0.471 -0.030 0.081  -0.040 249 GLN   AAA CB  
1950 C  CG  . GLN   A 250 ? 0.352 0.106 0.474 0.018  0.037  -0.056 249 GLN   AAA CG  
1951 C  CD  . GLN   A 250 ? 0.378 0.063 0.503 -0.066 0.022  -0.030 249 GLN   AAA CD  
1952 O  OE1 . GLN   A 250 ? 0.422 0.122 0.529 -0.014 -0.013 -0.030 249 GLN   AAA OE1 
1953 N  NE2 . GLN   A 250 ? 0.405 0.128 0.445 -0.121 0.072  -0.012 249 GLN   AAA NE2 
1954 N  N   . PRO   A 251 ? 0.451 0.240 0.572 -0.151 0.054  -0.031 250 PRO   AAA N   
1955 C  CA  . PRO   A 251 ? 0.430 0.189 0.581 -0.136 0.031  -0.063 250 PRO   AAA CA  
1956 C  C   . PRO   A 251 ? 0.362 0.185 0.469 -0.075 0.108  -0.065 250 PRO   AAA C   
1957 O  O   . PRO   A 251 ? 0.434 0.134 0.524 -0.011 0.095  -0.084 250 PRO   AAA O   
1958 C  CB  . PRO   A 251 ? 0.503 0.179 0.627 -0.149 0.039  -0.030 250 PRO   AAA CB  
1959 C  CG  . PRO   A 251 ? 0.564 0.124 0.581 -0.178 0.078  -0.118 250 PRO   AAA CG  
1960 C  CD  . PRO   A 251 ? 0.553 0.026 0.607 -0.045 0.081  -0.104 250 PRO   AAA CD  
1961 N  N   . LEU   A 252 ? 0.472 0.104 0.454 -0.075 0.071  -0.111 251 LEU   AAA N   
1962 C  CA  . LEU   A 252 ? 0.511 0.164 0.519 -0.110 0.033  -0.157 251 LEU   AAA CA  
1963 C  C   . LEU   A 252 ? 0.454 0.256 0.587 -0.070 0.020  -0.018 251 LEU   AAA C   
1964 O  O   . LEU   A 252 ? 0.508 0.145 0.649 -0.032 0.047  -0.124 251 LEU   AAA O   
1965 C  CB  . LEU   A 252 ? 0.595 0.276 0.554 -0.159 0.069  -0.207 251 LEU   AAA CB  
1966 C  CG  . LEU   A 252 ? 0.703 0.239 0.631 -0.105 0.171  0.024  251 LEU   AAA CG  
1967 C  CD1 . LEU   A 252 ? 0.885 0.291 0.686 -0.127 0.221  0.067  251 LEU   AAA CD1 
1968 C  CD2 . LEU   A 252 ? 0.577 0.280 0.495 -0.156 0.000  -0.119 251 LEU   AAA CD2 
1969 N  N   . LYS   A 253 ? 0.522 0.226 0.610 -0.072 0.044  -0.179 252 LYS   AAA N   
1970 C  CA  . LYS   A 253 ? 0.478 0.216 0.640 -0.041 0.006  -0.089 252 LYS   AAA CA  
1971 C  C   . LYS   A 253 ? 0.457 0.095 0.573 -0.123 0.019  -0.040 252 LYS   AAA C   
1972 O  O   . LYS   A 253 ? 0.442 0.281 0.745 -0.108 -0.035 -0.141 252 LYS   AAA O   
1973 C  CB  . LYS   A 253 ? 0.478 0.174 0.640 -0.149 -0.035 -0.130 252 LYS   AAA CB  
1974 C  CG  . LYS   A 253 ? 0.459 0.241 0.718 -0.095 -0.106 -0.153 252 LYS   AAA CG  
1975 C  CD  . LYS   A 253 ? 0.581 0.341 0.761 -0.114 -0.106 -0.001 252 LYS   AAA CD  
1976 C  CE  . LYS   A 253 ? 0.833 0.497 0.797 -0.045 -0.094 0.183  252 LYS   AAA CE  
1977 N  NZ  . LYS   A 253 ? 1.014 0.632 0.985 -0.151 -0.013 0.157  252 LYS   AAA NZ  
1978 N  N   . GLY   A 254 ? 0.407 0.281 0.598 -0.072 -0.002 -0.084 253 GLY   AAA N   
1979 C  CA  . GLY   A 254 ? 0.433 0.323 0.655 -0.061 -0.026 -0.095 253 GLY   AAA CA  
1980 C  C   . GLY   A 254 ? 0.489 0.321 0.524 -0.098 -0.076 -0.129 253 GLY   AAA C   
1981 O  O   . GLY   A 254 ? 0.542 0.239 0.542 -0.130 -0.088 -0.082 253 GLY   AAA O   
1982 N  N   . ARG   A 255 ? 0.442 0.154 0.602 -0.081 -0.022 -0.130 254 ARG   AAA N   
1983 C  CA  . ARG   A 255 ? 0.473 0.162 0.494 -0.117 -0.028 -0.085 254 ARG   AAA CA  
1984 C  C   . ARG   A 255 ? 0.519 0.209 0.488 -0.020 0.005  -0.082 254 ARG   AAA C   
1985 O  O   . ARG   A 255 ? 0.479 0.276 0.547 -0.088 0.055  -0.182 254 ARG   AAA O   
1986 C  CB  . ARG   A 255 ? 0.411 0.233 0.479 -0.113 0.015  -0.117 254 ARG   AAA CB  
1987 C  CG  . ARG   A 255 ? 0.463 0.216 0.463 -0.066 0.038  -0.137 254 ARG   AAA CG  
1988 C  CD  . ARG   A 255 ? 0.390 0.173 0.477 -0.071 0.015  -0.090 254 ARG   AAA CD  
1989 N  NE  . ARG   A 255 ? 0.438 0.065 0.529 -0.110 -0.009 -0.126 254 ARG   AAA NE  
1990 C  CZ  . ARG   A 255 ? 0.332 0.112 0.466 -0.052 0.022  -0.132 254 ARG   AAA CZ  
1991 N  NH1 . ARG   A 255 ? 0.419 0.128 0.509 -0.081 0.012  -0.161 254 ARG   AAA NH1 
1992 N  NH2 . ARG   A 255 ? 0.352 0.032 0.523 -0.084 0.048  -0.062 254 ARG   AAA NH2 
1993 N  N   . THR   A 256 ? 0.451 0.169 0.503 -0.081 -0.010 -0.082 255 THR   AAA N   
1994 C  CA  . THR   A 256 ? 0.556 0.090 0.501 -0.146 -0.038 -0.091 255 THR   AAA CA  
1995 C  C   . THR   A 256 ? 0.400 0.132 0.470 -0.137 0.026  -0.105 255 THR   AAA C   
1996 O  O   . THR   A 256 ? 0.448 0.290 0.517 -0.038 -0.001 -0.170 255 THR   AAA O   
1997 C  CB  . THR   A 256 ? 0.529 0.447 0.477 -0.129 -0.058 -0.093 255 THR   AAA CB  
1998 O  OG1 . THR   A 256 ? 0.568 0.455 0.578 -0.243 -0.043 -0.016 255 THR   AAA OG1 
1999 C  CG2 . THR   A 256 ? 0.497 0.556 0.578 -0.202 -0.018 -0.062 255 THR   AAA CG2 
2000 N  N   . VAL   A 257 ? 0.392 0.202 0.468 -0.121 0.021  -0.100 256 VAL   AAA N   
2001 C  CA  . VAL   A 257 ? 0.343 0.230 0.464 -0.109 -0.013 -0.147 256 VAL   AAA CA  
2002 C  C   . VAL   A 257 ? 0.463 0.227 0.456 -0.025 -0.036 -0.157 256 VAL   AAA C   
2003 O  O   . VAL   A 257 ? 0.432 0.118 0.466 -0.073 0.000  -0.094 256 VAL   AAA O   
2004 C  CB  . VAL   A 257 ? 0.364 0.306 0.447 -0.109 -0.018 -0.148 256 VAL   AAA CB  
2005 C  CG1 . VAL   A 257 ? 0.335 0.153 0.457 -0.008 0.029  -0.132 256 VAL   AAA CG1 
2006 C  CG2 . VAL   A 257 ? 0.454 0.250 0.493 -0.100 -0.048 -0.152 256 VAL   AAA CG2 
2007 N  N   . ARG   A 258 ? 0.390 0.260 0.414 -0.001 -0.001 -0.142 257 ARG   AAA N   
2008 C  CA  . ARG   A 258 ? 0.338 0.296 0.407 -0.034 -0.017 -0.132 257 ARG   AAA CA  
2009 C  C   . ARG   A 258 ? 0.393 0.051 0.409 0.031  -0.002 -0.069 257 ARG   AAA C   
2010 O  O   . ARG   A 258 ? 0.395 0.345 0.394 -0.010 0.011  -0.091 257 ARG   AAA O   
2011 C  CB  . ARG   A 258 ? 0.399 0.169 0.467 -0.020 -0.001 -0.131 257 ARG   AAA CB  
2012 C  CG  . ARG   A 258 ? 0.383 0.358 0.499 -0.063 0.028  -0.144 257 ARG   AAA CG  
2013 C  CD  . ARG   A 258 ? 0.455 0.334 0.498 0.004  0.043  -0.053 257 ARG   AAA CD  
2014 N  NE  . ARG   A 258 ? 0.412 0.386 0.505 -0.009 -0.022 -0.134 257 ARG   AAA NE  
2015 C  CZ  . ARG   A 258 ? 0.381 0.340 0.484 -0.020 -0.051 -0.035 257 ARG   AAA CZ  
2016 N  NH1 . ARG   A 258 ? 0.508 0.376 0.555 0.021  -0.109 -0.041 257 ARG   AAA NH1 
2017 N  NH2 . ARG   A 258 ? 0.392 0.425 0.523 0.016  -0.002 -0.091 257 ARG   AAA NH2 
2018 N  N   . ALA   A 259 ? 0.345 0.267 0.398 0.004  -0.006 -0.062 258 ALA   AAA N   
2019 C  CA  . ALA   A 259 ? 0.342 0.332 0.423 -0.020 0.004  -0.042 258 ALA   AAA CA  
2020 C  C   . ALA   A 259 ? 0.311 0.284 0.461 -0.044 -0.041 -0.089 258 ALA   AAA C   
2021 O  O   . ALA   A 259 ? 0.382 0.312 0.457 0.054  -0.074 -0.080 258 ALA   AAA O   
2022 C  CB  . ALA   A 259 ? 0.343 0.278 0.475 -0.036 -0.010 -0.109 258 ALA   AAA CB  
2023 N  N   . SER   A 260 ? 0.382 0.171 0.428 0.022  -0.076 -0.038 259 SER   AAA N   
2024 C  CA  . SER   A 260 ? 0.414 0.230 0.421 0.044  -0.067 0.020  259 SER   AAA CA  
2025 C  C   . SER   A 260 ? 0.420 0.388 0.397 0.039  -0.051 -0.060 259 SER   AAA C   
2026 O  O   . SER   A 260 ? 0.412 0.433 0.425 0.035  -0.038 -0.010 259 SER   AAA O   
2027 C  CB  . SER   A 260 ? 0.398 0.285 0.402 0.068  -0.107 0.001  259 SER   AAA CB  
2028 O  OG  . SER   A 260 ? 0.383 0.312 0.442 0.023  -0.065 -0.083 259 SER   AAA OG  
2029 N  N   . PHE   A 261 ? 0.393 0.358 0.472 0.011  -0.010 -0.030 260 PHE   AAA N   
2030 C  CA  . PHE   A 261 ? 0.411 0.370 0.446 0.094  0.004  -0.093 260 PHE   AAA CA  
2031 C  C   . PHE   A 261 ? 0.523 0.418 0.486 -0.021 0.025  -0.152 260 PHE   AAA C   
2032 O  O   . PHE   A 261 ? 0.568 0.483 0.507 -0.078 0.032  -0.209 260 PHE   AAA O   
2033 C  CB  . PHE   A 261 ? 0.422 0.390 0.475 0.055  -0.003 -0.019 260 PHE   AAA CB  
2034 C  CG  . PHE   A 261 ? 0.445 0.235 0.467 0.051  0.011  -0.094 260 PHE   AAA CG  
2035 C  CD1 . PHE   A 261 ? 0.347 0.305 0.421 0.020  -0.036 -0.090 260 PHE   AAA CD1 
2036 C  CD2 . PHE   A 261 ? 0.434 0.490 0.457 0.152  0.042  -0.049 260 PHE   AAA CD2 
2037 C  CE1 . PHE   A 261 ? 0.391 0.403 0.385 0.034  -0.016 -0.077 260 PHE   AAA CE1 
2038 C  CE2 . PHE   A 261 ? 0.492 0.484 0.494 0.088  -0.000 -0.017 260 PHE   AAA CE2 
2039 C  CZ  . PHE   A 261 ? 0.374 0.375 0.470 0.061  -0.020 -0.063 260 PHE   AAA CZ  
2040 O  OXT . PHE   A 261 ? 0.531 0.389 0.472 0.025  0.051  -0.081 260 PHE   AAA OXT 
2041 N  N   . SER   B 3   ? 0.847 0.475 0.872 0.230  -0.298 -0.360 2   SER   BBB N   
2042 C  CA  . SER   B 3   ? 0.814 0.404 0.725 0.083  -0.042 -0.114 2   SER   BBB CA  
2043 C  C   . SER   B 3   ? 0.542 0.390 0.793 0.034  -0.132 -0.151 2   SER   BBB C   
2044 O  O   . SER   B 3   ? 0.516 0.250 0.780 -0.017 -0.024 -0.058 2   SER   BBB O   
2045 C  CB  . SER   B 3   ? 0.667 0.266 0.863 0.012  -0.065 -0.176 2   SER   BBB CB  
2046 O  OG  . SER   B 3   ? 0.537 0.811 1.064 -0.185 0.170  -0.146 2   SER   BBB OG  
2047 N  N   . PRO   B 4   ? 0.593 0.441 0.740 -0.130 -0.096 0.044  3   PRO   BBB N   
2048 C  CA  . PRO   B 4   ? 0.583 0.441 0.754 -0.049 -0.002 0.061  3   PRO   BBB CA  
2049 C  C   . PRO   B 4   ? 0.670 0.121 0.829 -0.235 -0.022 -0.052 3   PRO   BBB C   
2050 O  O   . PRO   B 4   ? 0.599 0.680 0.662 -0.037 0.142  0.025  3   PRO   BBB O   
2051 C  CB  . PRO   B 4   ? 0.618 0.495 0.851 -0.214 -0.087 0.060  3   PRO   BBB CB  
2052 C  CG  . PRO   B 4   ? 0.544 0.664 0.750 -0.137 0.050  0.131  3   PRO   BBB CG  
2053 C  CD  . PRO   B 4   ? 0.467 0.592 0.777 -0.160 -0.029 0.068  3   PRO   BBB CD  
2054 N  N   . ASP   B 5   ? 0.752 0.102 0.817 -0.255 0.078  -0.020 4   ASP   BBB N   
2055 C  CA  . ASP   B 5   ? 0.603 0.195 0.666 -0.113 -0.040 -0.028 4   ASP   BBB CA  
2056 C  C   . ASP   B 5   ? 0.577 0.058 0.659 0.005  0.028  -0.061 4   ASP   BBB C   
2057 O  O   . ASP   B 5   ? 0.694 0.029 0.757 -0.086 0.050  -0.101 4   ASP   BBB O   
2058 C  CB  . ASP   B 5   ? 0.618 0.247 0.709 -0.022 0.015  -0.102 4   ASP   BBB CB  
2059 C  CG  . ASP   B 5   ? 0.654 0.595 0.878 -0.097 0.095  -0.172 4   ASP   BBB CG  
2060 O  OD1 . ASP   B 5   ? 0.478 0.493 0.767 -0.115 -0.030 -0.208 4   ASP   BBB OD1 
2061 O  OD2 . ASP   B 5   ? 0.748 0.650 1.145 -0.355 0.085  -0.258 4   ASP   BBB OD2 
2062 N  N   . TRP   B 6   ? 0.455 0.189 0.495 -0.049 0.042  -0.068 5   TRP   BBB N   
2063 C  CA  . TRP   B 6   ? 0.399 0.121 0.492 -0.035 0.010  -0.042 5   TRP   BBB CA  
2064 C  C   . TRP   B 6   ? 0.449 0.199 0.428 0.025  0.009  -0.043 5   TRP   BBB C   
2065 O  O   . TRP   B 6   ? 0.462 0.214 0.530 -0.053 -0.043 0.030  5   TRP   BBB O   
2066 C  CB  . TRP   B 6   ? 0.335 0.219 0.528 -0.039 0.015  -0.031 5   TRP   BBB CB  
2067 C  CG  . TRP   B 6   ? 0.382 0.200 0.499 0.058  0.072  -0.099 5   TRP   BBB CG  
2068 C  CD1 . TRP   B 6   ? 0.401 0.222 0.481 0.024  0.036  -0.108 5   TRP   BBB CD1 
2069 C  CD2 . TRP   B 6   ? 0.303 0.099 0.442 0.028  0.010  -0.075 5   TRP   BBB CD2 
2070 N  NE1 . TRP   B 6   ? 0.390 0.154 0.513 0.088  0.033  -0.008 5   TRP   BBB NE1 
2071 C  CE2 . TRP   B 6   ? 0.288 0.137 0.506 -0.007 0.029  -0.087 5   TRP   BBB CE2 
2072 C  CE3 . TRP   B 6   ? 0.363 0.145 0.434 0.003  0.022  -0.060 5   TRP   BBB CE3 
2073 C  CZ2 . TRP   B 6   ? 0.315 0.146 0.508 0.097  0.028  -0.033 5   TRP   BBB CZ2 
2074 C  CZ3 . TRP   B 6   ? 0.331 0.111 0.486 -0.056 0.004  -0.082 5   TRP   BBB CZ3 
2075 C  CH2 . TRP   B 6   ? 0.323 0.032 0.490 0.061  0.034  -0.077 5   TRP   BBB CH2 
2076 N  N   . GLY   B 7   ? 0.441 0.063 0.528 0.056  0.037  -0.031 6   GLY   BBB N   
2077 C  CA  . GLY   B 7   ? 0.385 0.159 0.525 -0.045 0.045  -0.089 6   GLY   BBB CA  
2078 C  C   . GLY   B 7   ? 0.384 0.206 0.427 -0.072 -0.044 -0.112 6   GLY   BBB C   
2079 O  O   . GLY   B 7   ? 0.359 0.080 0.483 0.007  -0.028 -0.097 6   GLY   BBB O   
2080 N  N   . TYR   B 8   ? 0.384 0.176 0.521 -0.038 -0.020 -0.138 7   TYR   BBB N   
2081 C  CA  . TYR   B 8   ? 0.381 0.178 0.573 -0.069 0.037  -0.147 7   TYR   BBB CA  
2082 C  C   . TYR   B 8   ? 0.453 0.219 0.722 -0.087 -0.014 -0.138 7   TYR   BBB C   
2083 O  O   . TYR   B 8   ? 0.578 0.076 0.711 -0.075 0.067  -0.153 7   TYR   BBB O   
2084 C  CB  . TYR   B 8   ? 0.366 0.139 0.576 -0.005 0.002  -0.084 7   TYR   BBB CB  
2085 C  CG  . TYR   B 8   ? 0.333 0.008 0.480 0.023  0.025  0.011  7   TYR   BBB CG  
2086 C  CD1 . TYR   B 8   ? 0.368 0.008 0.488 0.024  0.010  0.012  7   TYR   BBB CD1 
2087 C  CD2 . TYR   B 8   ? 0.345 0.021 0.464 -0.002 -0.024 0.075  7   TYR   BBB CD2 
2088 C  CE1 . TYR   B 8   ? 0.379 0.013 0.435 0.045  0.029  -0.020 7   TYR   BBB CE1 
2089 C  CE2 . TYR   B 8   ? 0.340 0.020 0.459 0.045  0.012  -0.058 7   TYR   BBB CE2 
2090 C  CZ  . TYR   B 8   ? 0.347 0.007 0.470 0.003  -0.027 0.011  7   TYR   BBB CZ  
2091 O  OH  . TYR   B 8   ? 0.305 0.006 0.483 0.002  0.010  0.006  7   TYR   BBB OH  
2092 N  N   . ASP   B 9   ? 0.560 0.033 0.787 -0.030 -0.035 -0.099 8   ASP   BBB N   
2093 C  CA  . ASP   B 9   ? 0.568 0.258 0.741 -0.194 -0.040 -0.093 8   ASP   BBB CA  
2094 C  C   . ASP   B 9   ? 0.559 0.242 0.784 -0.233 -0.012 -0.065 8   ASP   BBB C   
2095 O  O   . ASP   B 9   ? 0.588 0.147 0.555 -0.103 0.058  -0.146 8   ASP   BBB O   
2096 C  CB  . ASP   B 9   ? 0.608 0.359 0.811 -0.111 -0.080 -0.062 8   ASP   BBB CB  
2097 C  CG  . ASP   B 9   ? 0.647 0.624 0.943 -0.103 -0.017 0.140  8   ASP   BBB CG  
2098 O  OD1 . ASP   B 9   ? 0.680 0.520 1.022 -0.052 0.195  -0.130 8   ASP   BBB OD1 
2099 O  OD2 . ASP   B 9   ? 0.756 0.988 0.976 -0.288 -0.024 0.384  8   ASP   BBB OD2 
2100 N  N   . ASP   B 10  ? 0.632 0.350 0.765 -0.333 0.061  -0.104 9   ASP   BBB N   
2101 C  CA  . ASP   B 10  ? 0.824 0.536 0.865 -0.065 -0.013 -0.013 9   ASP   BBB CA  
2102 C  C   . ASP   B 10  ? 1.013 0.649 1.050 0.048  0.282  0.034  9   ASP   BBB C   
2103 O  O   . ASP   B 10  ? 1.473 0.925 1.740 -0.643 -0.682 -0.134 9   ASP   BBB O   
2104 C  CB  . ASP   B 10  ? 0.979 0.375 0.900 -0.111 0.077  0.058  9   ASP   BBB CB  
2105 N  N   . LYS   B 11  ? 0.806 0.555 1.018 0.036  0.008  -0.243 10  LYS   BBB N   
2106 C  CA  . LYS   B 11  ? 0.795 0.036 0.873 -0.088 -0.119 -0.039 10  LYS   BBB CA  
2107 C  C   . LYS   B 11  ? 0.605 0.242 0.827 0.015  -0.041 -0.136 10  LYS   BBB C   
2108 O  O   . LYS   B 11  ? 0.720 0.224 0.730 0.030  0.112  -0.197 10  LYS   BBB O   
2109 C  CB  . LYS   B 11  ? 0.737 0.470 0.874 -0.049 -0.041 0.090  10  LYS   BBB CB  
2110 C  CG  . LYS   B 11  ? 0.906 0.783 0.904 0.035  0.111  -0.025 10  LYS   BBB CG  
2111 C  CD  . LYS   B 11  ? 0.982 0.961 0.857 0.091  0.138  0.062  10  LYS   BBB CD  
2112 C  CE  . LYS   B 11  ? 1.129 0.904 0.923 0.039  0.132  0.017  10  LYS   BBB CE  
2113 N  NZ  . LYS   B 11  ? 1.125 0.785 1.005 0.123  0.209  -0.039 10  LYS   BBB NZ  
2114 N  N   . ASN   B 12  ? 0.583 0.265 0.626 -0.019 -0.040 -0.186 11  ASN   BBB N   
2115 C  CA  . ASN   B 12  ? 0.658 0.261 0.512 -0.060 -0.002 -0.098 11  ASN   BBB CA  
2116 C  C   . ASN   B 12  ? 0.515 0.160 0.505 -0.041 0.010  -0.060 11  ASN   BBB C   
2117 O  O   . ASN   B 12  ? 0.541 0.169 0.591 -0.067 0.044  -0.116 11  ASN   BBB O   
2118 C  CB  . ASN   B 12  ? 0.552 0.296 0.513 -0.012 -0.024 -0.102 11  ASN   BBB CB  
2119 C  CG  . ASN   B 12  ? 0.621 0.181 0.564 -0.006 -0.034 -0.060 11  ASN   BBB CG  
2120 O  OD1 . ASN   B 12  ? 0.557 0.207 0.588 0.054  -0.043 -0.088 11  ASN   BBB OD1 
2121 N  ND2 . ASN   B 12  ? 0.620 0.305 0.507 0.002  -0.156 -0.088 11  ASN   BBB ND2 
2122 N  N   . GLY   B 13  ? 0.491 0.072 0.559 0.016  0.059  -0.036 12  GLY   BBB N   
2123 C  CA  . GLY   B 13  ? 0.498 0.123 0.559 0.070  0.033  -0.018 12  GLY   BBB CA  
2124 C  C   . GLY   B 13  ? 0.440 0.204 0.477 -0.064 0.050  0.000  12  GLY   BBB C   
2125 O  O   . GLY   B 13  ? 0.471 0.073 0.654 0.018  0.102  0.009  12  GLY   BBB O   
2126 N  N   . PRO   B 14  ? 0.513 0.089 0.507 -0.001 0.080  -0.068 13  PRO   BBB N   
2127 C  CA  . PRO   B 14  ? 0.440 0.121 0.577 0.009  0.075  -0.011 13  PRO   BBB CA  
2128 C  C   . PRO   B 14  ? 0.405 0.120 0.628 0.020  0.090  -0.036 13  PRO   BBB C   
2129 O  O   . PRO   B 14  ? 0.457 0.080 0.577 -0.000 0.046  -0.104 13  PRO   BBB O   
2130 C  CB  . PRO   B 14  ? 0.440 0.142 0.562 0.014  0.067  -0.050 13  PRO   BBB CB  
2131 C  CG  . PRO   B 14  ? 0.416 0.075 0.512 -0.074 0.076  -0.014 13  PRO   BBB CG  
2132 C  CD  . PRO   B 14  ? 0.447 0.263 0.505 -0.003 0.105  -0.060 13  PRO   BBB CD  
2133 N  N   . GLU   B 15  ? 0.580 0.127 0.670 -0.011 0.075  -0.178 14  GLU   BBB N   
2134 C  CA  . GLU   B 15  ? 0.602 0.144 0.734 -0.043 0.140  -0.029 14  GLU   BBB CA  
2135 C  C   . GLU   B 15  ? 0.550 0.214 0.675 -0.056 0.055  -0.087 14  GLU   BBB C   
2136 O  O   . GLU   B 15  ? 0.576 0.112 0.797 0.039  0.118  0.009  14  GLU   BBB O   
2137 C  CB  . GLU   B 15  ? 0.610 0.125 0.740 -0.048 0.163  -0.096 14  GLU   BBB CB  
2138 C  CG  . GLU   B 15  ? 0.772 0.359 0.783 -0.036 0.230  -0.145 14  GLU   BBB CG  
2139 C  CD  . GLU   B 15  ? 0.935 0.442 0.854 -0.058 0.162  -0.138 14  GLU   BBB CD  
2140 O  OE1 . GLU   B 15  ? 0.967 0.362 0.883 -0.246 0.143  -0.246 14  GLU   BBB OE1 
2141 O  OE2 . GLU   B 15  ? 0.909 0.445 0.879 -0.049 0.206  -0.124 14  GLU   BBB OE2 
2142 N  N   . GLN   B 16  ? 0.532 0.023 0.701 -0.002 0.071  -0.104 15  GLN   BBB N   
2143 C  CA  . GLN   B 16  ? 0.510 0.185 0.777 -0.077 0.115  -0.086 15  GLN   BBB CA  
2144 C  C   . GLN   B 16  ? 0.559 0.097 0.569 -0.036 0.060  -0.121 15  GLN   BBB C   
2145 O  O   . GLN   B 16  ? 0.480 0.131 0.573 -0.016 0.068  -0.096 15  GLN   BBB O   
2146 C  CB  . GLN   B 16  ? 0.719 0.310 0.780 0.096  0.080  -0.145 15  GLN   BBB CB  
2147 C  CG  . GLN   B 16  ? 0.867 0.842 0.901 -0.137 -0.089 -0.167 15  GLN   BBB CG  
2148 C  CD  . GLN   B 16  ? 1.103 0.836 0.897 -0.145 -0.135 0.157  15  GLN   BBB CD  
2149 O  OE1 . GLN   B 16  ? 1.631 0.337 1.562 0.374  -0.254 -0.050 15  GLN   BBB OE1 
2150 N  NE2 . GLN   B 16  ? 0.815 0.439 1.108 -0.076 -0.161 -0.001 15  GLN   BBB NE2 
2151 N  N   . TRP   B 17  ? 0.476 0.022 0.525 -0.009 0.081  -0.060 16  TRP   BBB N   
2152 C  CA  . TRP   B 17  ? 0.425 0.026 0.496 0.011  0.057  -0.039 16  TRP   BBB CA  
2153 C  C   . TRP   B 17  ? 0.475 0.142 0.533 0.104  0.108  -0.077 16  TRP   BBB C   
2154 O  O   . TRP   B 17  ? 0.514 0.056 0.622 0.116  0.141  -0.039 16  TRP   BBB O   
2155 C  CB  . TRP   B 17  ? 0.421 0.139 0.518 0.074  0.045  -0.096 16  TRP   BBB CB  
2156 C  CG  . TRP   B 17  ? 0.430 0.058 0.446 0.047  0.031  -0.080 16  TRP   BBB CG  
2157 C  CD1 . TRP   B 17  ? 0.431 0.015 0.485 0.047  0.004  -0.039 16  TRP   BBB CD1 
2158 C  CD2 . TRP   B 17  ? 0.409 0.007 0.455 -0.002 0.031  -0.020 16  TRP   BBB CD2 
2159 N  NE1 . TRP   B 17  ? 0.455 0.042 0.446 0.091  0.005  -0.087 16  TRP   BBB NE1 
2160 C  CE2 . TRP   B 17  ? 0.407 0.018 0.470 -0.003 0.015  -0.072 16  TRP   BBB CE2 
2161 C  CE3 . TRP   B 17  ? 0.401 0.008 0.443 0.007  0.035  -0.023 16  TRP   BBB CE3 
2162 C  CZ2 . TRP   B 17  ? 0.460 0.017 0.464 0.071  0.033  0.005  16  TRP   BBB CZ2 
2163 C  CZ3 . TRP   B 17  ? 0.418 0.013 0.431 -0.023 -0.003 -0.049 16  TRP   BBB CZ3 
2164 C  CH2 . TRP   B 17  ? 0.428 0.007 0.484 -0.019 0.011  0.006  16  TRP   BBB CH2 
2165 N  N   . SER   B 18  ? 0.481 0.241 0.487 0.019  0.099  0.012  17  SER   BBB N   
2166 C  CA  . SER   B 18  ? 0.484 0.231 0.541 -0.030 0.070  0.038  17  SER   BBB CA  
2167 C  C   . SER   B 18  ? 0.567 0.019 0.511 -0.061 0.018  -0.003 17  SER   BBB C   
2168 O  O   . SER   B 18  ? 0.551 0.092 0.538 0.047  0.062  -0.003 17  SER   BBB O   
2169 C  CB  . SER   B 18  ? 0.549 0.120 0.620 -0.055 0.022  0.009  17  SER   BBB CB  
2170 O  OG  . SER   B 18  ? 0.650 0.008 0.770 0.030  0.189  -0.004 17  SER   BBB OG  
2171 N  N   . LYS   B 19  ? 0.555 0.056 0.509 -0.057 0.073  0.021  18  LYS   BBB N   
2172 C  CA  . LYS   B 19  ? 0.511 0.200 0.551 -0.006 0.120  0.027  18  LYS   BBB CA  
2173 C  C   . LYS   B 19  ? 0.566 0.209 0.712 -0.023 0.105  -0.010 18  LYS   BBB C   
2174 O  O   . LYS   B 19  ? 0.561 0.021 0.673 0.003  0.037  -0.099 18  LYS   BBB O   
2175 C  CB  . LYS   B 19  ? 0.454 0.167 0.635 -0.017 0.121  -0.010 18  LYS   BBB CB  
2176 C  CG  . LYS   B 19  ? 0.529 0.267 0.744 -0.140 0.158  -0.035 18  LYS   BBB CG  
2177 C  CD  . LYS   B 19  ? 0.798 0.504 0.861 -0.193 0.043  -0.167 18  LYS   BBB CD  
2178 C  CE  . LYS   B 19  ? 0.887 0.370 0.947 -0.231 -0.009 -0.228 18  LYS   BBB CE  
2179 N  NZ  . LYS   B 19  ? 0.987 0.683 1.022 -0.444 0.028  -0.270 18  LYS   BBB NZ  
2180 N  N   . LEU   B 20  ? 0.509 0.136 0.602 -0.060 0.070  -0.002 19  LEU   BBB N   
2181 C  CA  . LEU   B 20  ? 0.398 0.166 0.565 -0.061 0.026  -0.001 19  LEU   BBB CA  
2182 C  C   . LEU   B 20  ? 0.371 0.097 0.470 0.134  0.062  -0.062 19  LEU   BBB C   
2183 O  O   . LEU   B 20  ? 0.487 0.260 0.631 0.044  0.186  -0.010 19  LEU   BBB O   
2184 C  CB  . LEU   B 20  ? 0.453 0.312 0.639 -0.021 -0.032 0.043  19  LEU   BBB CB  
2185 C  CG  . LEU   B 20  ? 0.634 0.425 0.662 -0.008 -0.118 0.067  19  LEU   BBB CG  
2186 C  CD1 . LEU   B 20  ? 0.796 0.571 0.789 0.072  -0.133 -0.163 19  LEU   BBB CD1 
2187 C  CD2 . LEU   B 20  ? 0.569 0.506 0.580 -0.077 -0.150 -0.048 19  LEU   BBB CD2 
2188 N  N   . TYR   B 21  ? 0.482 0.031 0.489 0.042  0.105  -0.049 20  TYR   BBB N   
2189 C  CA  . TYR   B 21  ? 0.433 0.098 0.433 0.163  0.069  -0.074 20  TYR   BBB CA  
2190 C  C   . TYR   B 21  ? 0.495 0.020 0.627 -0.062 0.052  0.050  20  TYR   BBB C   
2191 O  O   . TYR   B 21  ? 0.525 0.031 0.600 0.076  0.107  -0.013 20  TYR   BBB O   
2192 C  CB  . TYR   B 21  ? 0.508 0.013 0.601 0.058  0.075  -0.005 20  TYR   BBB CB  
2193 C  CG  . TYR   B 21  ? 0.400 0.233 0.445 0.120  0.113  0.061  20  TYR   BBB CG  
2194 C  CD1 . TYR   B 21  ? 0.514 0.155 0.530 0.083  0.113  -0.003 20  TYR   BBB CD1 
2195 C  CD2 . TYR   B 21  ? 0.456 0.125 0.524 0.032  0.071  -0.004 20  TYR   BBB CD2 
2196 C  CE1 . TYR   B 21  ? 0.529 0.311 0.490 0.076  0.064  -0.005 20  TYR   BBB CE1 
2197 C  CE2 . TYR   B 21  ? 0.618 0.050 0.572 0.093  0.138  -0.030 20  TYR   BBB CE2 
2198 C  CZ  . TYR   B 21  ? 0.529 0.183 0.497 0.047  0.082  -0.035 20  TYR   BBB CZ  
2199 O  OH  . TYR   B 21  ? 0.599 0.187 0.643 -0.012 0.017  0.030  20  TYR   BBB OH  
2200 N  N   . PRO   B 22  ? 0.541 0.210 0.588 0.083  0.091  0.134  21  PRO   BBB N   
2201 C  CA  . PRO   B 22  ? 0.535 0.150 0.552 0.072  0.060  0.091  21  PRO   BBB CA  
2202 C  C   . PRO   B 22  ? 0.420 0.178 0.581 0.003  0.003  0.062  21  PRO   BBB C   
2203 O  O   . PRO   B 22  ? 0.476 0.130 0.540 0.108  0.062  0.040  21  PRO   BBB O   
2204 C  CB  . PRO   B 22  ? 0.545 0.144 0.655 0.199  0.040  0.041  21  PRO   BBB CB  
2205 C  CG  . PRO   B 22  ? 0.629 0.144 0.733 0.287  0.079  0.061  21  PRO   BBB CG  
2206 C  CD  . PRO   B 22  ? 0.602 0.083 0.684 0.141  0.150  0.183  21  PRO   BBB CD  
2207 N  N   . ILE   B 23  ? 0.444 0.116 0.601 0.054  0.059  0.038  22  ILE   BBB N   
2208 C  CA  . ILE   B 23  ? 0.395 0.041 0.588 -0.072 0.007  0.048  22  ILE   BBB CA  
2209 C  C   . ILE   B 23  ? 0.410 0.072 0.531 0.028  0.031  0.088  22  ILE   BBB C   
2210 O  O   . ILE   B 23  ? 0.473 0.172 0.567 0.050  0.096  0.031  22  ILE   BBB O   
2211 C  CB  . ILE   B 23  ? 0.302 0.012 0.631 -0.012 0.020  0.058  22  ILE   BBB CB  
2212 C  CG1 . ILE   B 23  ? 0.414 0.165 0.582 0.068  0.040  0.027  22  ILE   BBB CG1 
2213 C  CG2 . ILE   B 23  ? 0.430 0.019 0.616 0.073  0.049  0.014  22  ILE   BBB CG2 
2214 C  CD1 . ILE   B 23  ? 0.429 0.344 0.706 0.081  0.032  0.076  22  ILE   BBB CD1 
2215 N  N   . ALA   B 24  ? 0.378 0.080 0.560 0.082  0.022  0.071  23  ALA   BBB N   
2216 C  CA  . ALA   B 24  ? 0.434 0.142 0.523 0.057  0.071  0.047  23  ALA   BBB CA  
2217 C  C   . ALA   B 24  ? 0.448 0.196 0.556 0.094  0.091  0.088  23  ALA   BBB C   
2218 O  O   . ALA   B 24  ? 0.489 0.061 0.565 0.057  0.098  0.073  23  ALA   BBB O   
2219 C  CB  . ALA   B 24  ? 0.534 0.014 0.670 0.048  0.045  -0.043 23  ALA   BBB CB  
2220 N  N   . ASN   B 25  ? 0.472 0.213 0.546 0.134  0.060  0.069  24  ASN   BBB N   
2221 C  CA  . ASN   B 25  ? 0.566 0.022 0.486 0.027  0.068  -0.078 24  ASN   BBB CA  
2222 C  C   . ASN   B 25  ? 0.529 0.075 0.467 0.017  0.020  0.067  24  ASN   BBB C   
2223 O  O   . ASN   B 25  ? 0.553 0.114 0.504 0.053  0.005  0.091  24  ASN   BBB O   
2224 C  CB  . ASN   B 25  ? 0.644 0.020 0.628 0.085  0.022  -0.037 24  ASN   BBB CB  
2225 C  CG  . ASN   B 25  ? 0.654 0.039 0.680 0.028  0.017  0.067  24  ASN   BBB CG  
2226 O  OD1 . ASN   B 25  ? 0.797 0.248 0.673 0.079  -0.003 -0.013 24  ASN   BBB OD1 
2227 N  ND2 . ASN   B 25  ? 0.754 0.010 0.673 0.042  0.153  0.032  24  ASN   BBB ND2 
2228 N  N   . GLY   B 26  ? 0.474 0.045 0.619 0.059  0.091  0.025  25  GLY   BBB N   
2229 C  CA  . GLY   B 26  ? 0.505 0.040 0.604 0.129  0.020  0.024  25  GLY   BBB CA  
2230 C  C   . GLY   B 26  ? 0.534 0.019 0.638 0.075  0.063  0.043  25  GLY   BBB C   
2231 O  O   . GLY   B 26  ? 0.499 0.083 0.606 0.049  0.083  0.041  25  GLY   BBB O   
2232 N  N   . ASN   B 27  ? 0.499 0.165 0.524 0.146  0.067  0.049  26  ASN   BBB N   
2233 C  CA  . ASN   B 27  ? 0.486 0.203 0.543 0.185  0.136  0.002  26  ASN   BBB CA  
2234 C  C   . ASN   B 27  ? 0.447 0.050 0.474 0.069  -0.003 0.062  26  ASN   BBB C   
2235 O  O   . ASN   B 27  ? 0.555 0.130 0.526 0.165  0.054  0.103  26  ASN   BBB O   
2236 C  CB  . ASN   B 27  ? 0.519 0.273 0.576 0.159  0.049  0.056  26  ASN   BBB CB  
2237 C  CG  . ASN   B 27  ? 0.431 0.242 0.600 0.087  0.009  0.053  26  ASN   BBB CG  
2238 O  OD1 . ASN   B 27  ? 0.619 0.101 0.747 0.053  0.004  0.052  26  ASN   BBB OD1 
2239 N  ND2 . ASN   B 27  ? 0.430 0.316 0.830 0.051  0.005  -0.039 26  ASN   BBB ND2 
2240 N  N   . ASN   B 28  ? 0.418 0.097 0.503 0.087  0.021  0.096  27  ASN   BBB N   
2241 C  CA  . ASN   B 28  ? 0.378 0.113 0.461 0.079  0.004  0.076  27  ASN   BBB CA  
2242 C  C   . ASN   B 28  ? 0.381 0.024 0.530 0.040  -0.019 0.083  27  ASN   BBB C   
2243 O  O   . ASN   B 28  ? 0.405 0.011 0.510 0.014  0.021  0.047  27  ASN   BBB O   
2244 C  CB  . ASN   B 28  ? 0.376 0.106 0.542 0.056  0.029  0.096  27  ASN   BBB CB  
2245 C  CG  . ASN   B 28  ? 0.394 0.269 0.505 -0.001 0.001  0.133  27  ASN   BBB CG  
2246 O  OD1 . ASN   B 28  ? 0.437 0.461 0.808 0.192  -0.057 0.114  27  ASN   BBB OD1 
2247 N  ND2 . ASN   B 28  ? 0.359 0.637 0.499 0.085  -0.034 0.084  27  ASN   BBB ND2 
2248 N  N   . GLN   B 29  ? 0.346 0.018 0.516 0.061  0.004  0.020  28  GLN   BBB N   
2249 C  CA  . GLN   B 29  ? 0.371 0.050 0.468 -0.005 0.009  0.045  28  GLN   BBB CA  
2250 C  C   . GLN   B 29  ? 0.386 0.012 0.480 0.012  0.005  0.049  28  GLN   BBB C   
2251 O  O   . GLN   B 29  ? 0.431 0.020 0.475 0.066  -0.010 0.036  28  GLN   BBB O   
2252 C  CB  . GLN   B 29  ? 0.342 0.017 0.492 0.019  0.017  0.060  28  GLN   BBB CB  
2253 C  CG  . GLN   B 29  ? 0.410 0.085 0.473 0.032  0.033  0.096  28  GLN   BBB CG  
2254 C  CD  . GLN   B 29  ? 0.403 0.008 0.480 0.007  0.058  0.025  28  GLN   BBB CD  
2255 O  OE1 . GLN   B 29  ? 0.378 0.044 0.482 0.025  0.002  0.032  28  GLN   BBB OE1 
2256 N  NE2 . GLN   B 29  ? 0.361 0.017 0.589 0.060  0.050  -0.001 28  GLN   BBB NE2 
2257 N  N   . SER   B 30  ? 0.315 0.026 0.546 0.005  0.043  0.104  29  SER   BBB N   
2258 C  CA  . SER   B 30  ? 0.318 0.025 0.484 -0.032 0.064  0.079  29  SER   BBB CA  
2259 C  C   . SER   B 30  ? 0.407 0.017 0.552 -0.032 0.013  0.064  29  SER   BBB C   
2260 O  O   . SER   B 30  ? 0.340 0.013 0.539 0.014  0.045  0.060  29  SER   BBB O   
2261 C  CB  . SER   B 30  ? 0.396 0.024 0.457 0.002  -0.002 0.089  29  SER   BBB CB  
2262 O  OG  . SER   B 30  ? 0.357 0.016 0.478 0.017  -0.010 0.064  29  SER   BBB OG  
2263 N  N   . PRO   B 31  ? 0.425 0.014 0.486 -0.001 0.003  0.059  30  PRO   BBB N   
2264 C  CA  . PRO   B 31  ? 0.320 0.027 0.458 -0.059 -0.014 0.067  30  PRO   BBB CA  
2265 C  C   . PRO   B 31  ? 0.318 0.011 0.402 -0.022 0.044  0.033  30  PRO   BBB C   
2266 O  O   . PRO   B 31  ? 0.369 0.007 0.487 0.001  0.025  -0.010 30  PRO   BBB O   
2267 C  CB  . PRO   B 31  ? 0.323 0.015 0.406 -0.045 0.025  0.026  30  PRO   BBB CB  
2268 C  CG  . PRO   B 31  ? 0.393 0.023 0.495 -0.080 0.018  -0.007 30  PRO   BBB CG  
2269 C  CD  . PRO   B 31  ? 0.398 0.007 0.522 -0.002 0.010  -0.016 30  PRO   BBB CD  
2270 N  N   . VAL   B 32  ? 0.378 0.013 0.406 -0.001 0.047  0.051  31  VAL   BBB N   
2271 C  CA  . VAL   B 32  ? 0.364 0.009 0.458 0.009  0.042  0.035  31  VAL   BBB CA  
2272 C  C   . VAL   B 32  ? 0.327 0.027 0.463 0.054  0.057  0.080  31  VAL   BBB C   
2273 O  O   . VAL   B 32  ? 0.373 0.007 0.504 0.018  0.007  0.002  31  VAL   BBB O   
2274 C  CB  . VAL   B 32  ? 0.394 0.012 0.510 -0.008 -0.005 0.054  31  VAL   BBB CB  
2275 C  CG1 . VAL   B 32  ? 0.406 0.020 0.616 0.021  0.035  0.088  31  VAL   BBB CG1 
2276 C  CG2 . VAL   B 32  ? 0.347 0.015 0.590 -0.042 0.016  0.045  31  VAL   BBB CG2 
2277 N  N   . ASP   B 33  ? 0.480 0.013 0.527 -0.014 0.010  0.057  32  ASP   BBB N   
2278 C  CA  . ASP   B 33  ? 0.436 0.007 0.619 0.002  0.046  -0.012 32  ASP   BBB CA  
2279 C  C   . ASP   B 33  ? 0.407 0.009 0.462 0.033  0.108  0.021  32  ASP   BBB C   
2280 O  O   . ASP   B 33  ? 0.439 0.078 0.518 0.058  -0.002 -0.014 32  ASP   BBB O   
2281 C  CB  . ASP   B 33  ? 0.486 0.010 0.531 -0.034 0.004  0.027  32  ASP   BBB CB  
2282 C  CG  . ASP   B 33  ? 0.406 0.086 0.472 0.022  -0.043 0.045  32  ASP   BBB CG  
2283 O  OD1 . ASP   B 33  ? 0.341 0.069 0.496 -0.027 0.047  0.072  32  ASP   BBB OD1 
2284 O  OD2 . ASP   B 33  ? 0.543 0.138 0.485 0.070  0.002  0.088  32  ASP   BBB OD2 
2285 N  N   . ILE   B 34  ? 0.450 0.013 0.540 0.047  0.013  0.033  33  ILE   BBB N   
2286 C  CA  . ILE   B 34  ? 0.374 0.022 0.487 0.064  0.037  0.053  33  ILE   BBB CA  
2287 C  C   . ILE   B 34  ? 0.353 0.025 0.486 -0.041 -0.005 0.043  33  ILE   BBB C   
2288 O  O   . ILE   B 34  ? 0.360 0.015 0.466 -0.042 0.008  0.038  33  ILE   BBB O   
2289 C  CB  . ILE   B 34  ? 0.386 0.007 0.455 0.016  0.017  -0.001 33  ILE   BBB CB  
2290 C  CG1 . ILE   B 34  ? 0.443 0.017 0.451 0.060  0.007  0.001  33  ILE   BBB CG1 
2291 C  CG2 . ILE   B 34  ? 0.409 0.040 0.423 -0.023 0.029  0.004  33  ILE   BBB CG2 
2292 C  CD1 . ILE   B 34  ? 0.398 0.012 0.477 -0.010 0.003  -0.022 33  ILE   BBB CD1 
2293 N  N   . LYS   B 35  ? 0.383 0.040 0.491 0.018  0.008  0.039  34  LYS   BBB N   
2294 C  CA  . LYS   B 35  ? 0.444 0.012 0.494 0.039  0.032  0.037  34  LYS   BBB CA  
2295 C  C   . LYS   B 35  ? 0.410 0.061 0.519 -0.098 0.010  0.068  34  LYS   BBB C   
2296 O  O   . LYS   B 35  ? 0.405 0.044 0.470 -0.043 -0.020 0.063  34  LYS   BBB O   
2297 C  CB  . LYS   B 35  ? 0.478 0.041 0.561 0.119  0.014  0.048  34  LYS   BBB CB  
2298 C  CG  . LYS   B 35  ? 0.558 0.210 0.622 0.070  -0.006 0.113  34  LYS   BBB CG  
2299 C  CD  . LYS   B 35  ? 0.923 0.200 0.907 0.031  -0.007 0.147  34  LYS   BBB CD  
2300 C  CE  . LYS   B 35  ? 1.121 0.412 1.026 -0.155 0.048  0.295  34  LYS   BBB CE  
2301 N  NZ  . LYS   B 35  ? 1.361 0.571 0.959 0.159  0.011  0.281  34  LYS   BBB NZ  
2302 N  N   . THR   B 36  ? 0.385 0.122 0.451 -0.105 -0.032 0.072  35  THR   BBB N   
2303 C  CA  . THR   B 36  ? 0.385 0.052 0.542 -0.086 -0.040 0.055  35  THR   BBB CA  
2304 C  C   . THR   B 36  ? 0.513 0.179 0.487 -0.096 -0.084 0.016  35  THR   BBB C   
2305 O  O   . THR   B 36  ? 0.508 0.205 0.539 -0.087 -0.092 0.005  35  THR   BBB O   
2306 C  CB  . THR   B 36  ? 0.382 0.137 0.476 -0.090 -0.026 -0.009 35  THR   BBB CB  
2307 O  OG1 . THR   B 36  ? 0.454 0.124 0.504 -0.084 0.044  0.029  35  THR   BBB OG1 
2308 C  CG2 . THR   B 36  ? 0.420 0.165 0.537 -0.072 -0.044 0.063  35  THR   BBB CG2 
2309 N  N   . SER   B 37  ? 0.486 0.191 0.513 -0.024 0.003  0.112  36  SER   BBB N   
2310 C  CA  . SER   B 37  ? 0.573 0.234 0.520 -0.083 -0.054 0.109  36  SER   BBB CA  
2311 C  C   . SER   B 37  ? 0.512 0.253 0.429 -0.141 -0.114 0.076  36  SER   BBB C   
2312 O  O   . SER   B 37  ? 0.544 0.267 0.475 0.004  -0.124 0.068  36  SER   BBB O   
2313 C  CB  . SER   B 37  ? 0.611 0.258 0.512 -0.095 -0.038 0.183  36  SER   BBB CB  
2314 O  OG  . SER   B 37  ? 0.533 0.229 0.582 -0.124 -0.026 0.133  36  SER   BBB OG  
2315 N  N   . GLU   B 38  ? 0.455 0.040 0.498 -0.052 -0.062 0.122  37  GLU   BBB N   
2316 C  CA  . GLU   B 38  ? 0.456 0.155 0.652 -0.032 -0.046 0.106  37  GLU   BBB CA  
2317 C  C   . GLU   B 38  ? 0.414 0.117 0.675 -0.003 0.010  0.037  37  GLU   BBB C   
2318 O  O   . GLU   B 38  ? 0.376 0.178 0.692 0.018  -0.063 0.060  37  GLU   BBB O   
2319 C  CB  . GLU   B 38  ? 0.494 0.242 0.582 -0.021 0.001  0.161  37  GLU   BBB CB  
2320 C  CG  . GLU   B 38  ? 0.472 0.300 0.870 -0.036 -0.052 0.269  37  GLU   BBB CG  
2321 C  CD  . GLU   B 38  ? 0.714 0.386 0.894 -0.157 -0.093 0.342  37  GLU   BBB CD  
2322 O  OE1 . GLU   B 38  ? 0.703 0.558 0.970 -0.132 -0.193 0.142  37  GLU   BBB OE1 
2323 O  OE2 . GLU   B 38  ? 0.662 0.906 1.253 -0.185 0.067  0.257  37  GLU   BBB OE2 
2324 N  N   . THR   B 39  ? 0.402 0.080 0.465 -0.020 -0.018 0.078  38  THR   BBB N   
2325 C  CA  . THR   B 39  ? 0.374 0.074 0.471 -0.016 0.004  0.045  38  THR   BBB CA  
2326 C  C   . THR   B 39  ? 0.353 0.132 0.480 -0.028 -0.001 0.100  38  THR   BBB C   
2327 O  O   . THR   B 39  ? 0.439 0.211 0.523 -0.069 -0.001 0.115  38  THR   BBB O   
2328 C  CB  . THR   B 39  ? 0.451 0.026 0.500 -0.032 0.007  0.089  38  THR   BBB CB  
2329 O  OG1 . THR   B 39  ? 0.443 0.009 0.459 -0.000 -0.022 0.021  38  THR   BBB OG1 
2330 C  CG2 . THR   B 39  ? 0.460 0.029 0.536 0.028  -0.011 0.105  38  THR   BBB CG2 
2331 N  N   . LYS   B 40  ? 0.378 0.048 0.509 -0.049 -0.020 0.056  39  LYS   BBB N   
2332 C  CA  . LYS   B 40  ? 0.474 0.021 0.587 -0.082 -0.054 0.021  39  LYS   BBB CA  
2333 C  C   . LYS   B 40  ? 0.382 0.014 0.454 0.002  -0.085 0.058  39  LYS   BBB C   
2334 O  O   . LYS   B 40  ? 0.361 0.009 0.490 0.016  -0.036 0.027  39  LYS   BBB O   
2335 C  CB  . LYS   B 40  ? 0.439 0.035 0.756 -0.087 -0.100 0.092  39  LYS   BBB CB  
2336 C  CG  . LYS   B 40  ? 0.479 0.018 0.730 -0.027 -0.091 0.092  39  LYS   BBB CG  
2337 C  CD  . LYS   B 40  ? 0.572 0.075 0.726 -0.031 -0.141 0.129  39  LYS   BBB CD  
2338 C  CE  . LYS   B 40  ? 0.735 0.089 0.827 -0.001 -0.131 0.101  39  LYS   BBB CE  
2339 N  NZ  . LYS   B 40  ? 0.848 0.059 0.894 -0.134 -0.077 0.117  39  LYS   BBB NZ  
2340 N  N   . HIS   B 41  ? 0.452 0.022 0.460 -0.055 -0.024 0.068  40  HIS   BBB N   
2341 C  CA  . HIS   B 41  ? 0.395 0.022 0.411 0.007  -0.031 0.078  40  HIS   BBB CA  
2342 C  C   . HIS   B 41  ? 0.425 0.138 0.406 -0.040 -0.026 0.079  40  HIS   BBB C   
2343 O  O   . HIS   B 41  ? 0.421 0.106 0.437 0.013  -0.011 0.052  40  HIS   BBB O   
2344 C  CB  . HIS   B 41  ? 0.366 0.059 0.424 0.023  -0.022 0.059  40  HIS   BBB CB  
2345 C  CG  . HIS   B 41  ? 0.372 0.063 0.484 0.010  -0.066 0.089  40  HIS   BBB CG  
2346 N  ND1 . HIS   B 41  ? 0.355 0.127 0.483 0.014  -0.008 0.046  40  HIS   BBB ND1 
2347 C  CD2 . HIS   B 41  ? 0.359 0.032 0.490 0.032  -0.035 0.052  40  HIS   BBB CD2 
2348 C  CE1 . HIS   B 41  ? 0.381 0.112 0.481 0.044  -0.000 0.017  40  HIS   BBB CE1 
2349 N  NE2 . HIS   B 41  ? 0.455 0.100 0.464 0.002  -0.021 -0.035 40  HIS   BBB NE2 
2350 N  N   . ASP   B 42  ? 0.389 0.052 0.387 -0.017 -0.060 0.042  41  ASP   BBB N   
2351 C  CA  . ASP   B 42  ? 0.379 0.168 0.417 -0.012 -0.035 0.022  41  ASP   BBB CA  
2352 C  C   . ASP   B 42  ? 0.400 0.151 0.366 0.003  -0.034 0.049  41  ASP   BBB C   
2353 O  O   . ASP   B 42  ? 0.396 0.122 0.444 -0.018 -0.037 0.061  41  ASP   BBB O   
2354 C  CB  . ASP   B 42  ? 0.423 0.069 0.422 -0.026 -0.037 0.026  41  ASP   BBB CB  
2355 C  CG  . ASP   B 42  ? 0.380 0.168 0.415 0.015  -0.028 0.042  41  ASP   BBB CG  
2356 O  OD1 . ASP   B 42  ? 0.438 0.290 0.427 -0.062 -0.090 0.052  41  ASP   BBB OD1 
2357 O  OD2 . ASP   B 42  ? 0.588 0.198 0.438 -0.086 0.048  0.018  41  ASP   BBB OD2 
2358 N  N   . THR   B 43  ? 0.379 0.039 0.378 0.035  -0.026 0.045  42  THR   BBB N   
2359 C  CA  . THR   B 43  ? 0.390 0.060 0.417 0.020  -0.019 0.020  42  THR   BBB CA  
2360 C  C   . THR   B 43  ? 0.349 0.025 0.412 0.079  -0.006 -0.002 42  THR   BBB C   
2361 O  O   . THR   B 43  ? 0.350 0.016 0.471 0.031  -0.054 0.051  42  THR   BBB O   
2362 C  CB  . THR   B 43  ? 0.349 0.146 0.418 -0.002 -0.008 0.032  42  THR   BBB CB  
2363 O  OG1 . THR   B 43  ? 0.326 0.081 0.431 -0.000 -0.019 0.039  42  THR   BBB OG1 
2364 C  CG2 . THR   B 43  ? 0.378 0.142 0.419 0.007  -0.038 0.040  42  THR   BBB CG2 
2365 N  N   . SER   B 44  ? 0.343 0.125 0.373 0.041  -0.025 -0.003 43  SER   BBB N   
2366 C  CA  . SER   B 44  ? 0.371 0.152 0.374 -0.001 -0.044 0.011  43  SER   BBB CA  
2367 C  C   . SER   B 44  ? 0.334 0.198 0.377 -0.043 -0.021 0.103  43  SER   BBB C   
2368 O  O   . SER   B 44  ? 0.399 0.100 0.427 -0.081 -0.004 0.061  43  SER   BBB O   
2369 C  CB  . SER   B 44  ? 0.409 0.305 0.374 0.011  -0.007 -0.009 43  SER   BBB CB  
2370 O  OG  . SER   B 44  ? 0.420 0.192 0.368 0.050  -0.034 0.028  43  SER   BBB OG  
2371 N  N   . LEU   B 45  ? 0.324 0.085 0.398 0.015  -0.046 0.037  44  LEU   BBB N   
2372 C  CA  . LEU   B 45  ? 0.326 0.068 0.439 0.042  -0.046 0.051  44  LEU   BBB CA  
2373 C  C   . LEU   B 45  ? 0.433 0.029 0.427 -0.045 -0.017 -0.002 44  LEU   BBB C   
2374 O  O   . LEU   B 45  ? 0.460 0.165 0.438 -0.023 -0.016 0.114  44  LEU   BBB O   
2375 C  CB  . LEU   B 45  ? 0.300 0.196 0.443 0.014  -0.020 0.021  44  LEU   BBB CB  
2376 C  CG  . LEU   B 45  ? 0.303 0.177 0.457 0.007  -0.027 0.024  44  LEU   BBB CG  
2377 C  CD1 . LEU   B 45  ? 0.334 0.055 0.566 0.031  -0.029 0.050  44  LEU   BBB CD1 
2378 C  CD2 . LEU   B 45  ? 0.365 0.174 0.457 -0.027 -0.026 0.013  44  LEU   BBB CD2 
2379 N  N   . LYS   B 46  ? 0.401 0.119 0.452 -0.052 -0.019 0.056  45  LYS   BBB N   
2380 C  CA  . LYS   B 46  ? 0.378 0.123 0.442 -0.041 -0.077 0.018  45  LYS   BBB CA  
2381 C  C   . LYS   B 46  ? 0.370 0.142 0.403 -0.025 -0.067 0.005  45  LYS   BBB C   
2382 O  O   . LYS   B 46  ? 0.368 0.050 0.461 0.056  -0.084 -0.007 45  LYS   BBB O   
2383 C  CB  . LYS   B 46  ? 0.491 0.126 0.477 -0.106 -0.088 0.028  45  LYS   BBB CB  
2384 C  CG  . LYS   B 46  ? 0.499 0.152 0.489 -0.117 -0.096 0.083  45  LYS   BBB CG  
2385 C  CD  . LYS   B 46  ? 0.495 0.141 0.513 -0.096 -0.029 0.069  45  LYS   BBB CD  
2386 C  CE  . LYS   B 46  ? 0.606 0.303 0.597 -0.118 -0.110 0.053  45  LYS   BBB CE  
2387 N  NZ  . LYS   B 46  ? 0.727 0.136 0.715 -0.074 -0.077 0.071  45  LYS   BBB NZ  
2388 N  N   . PRO   B 47  ? 0.430 0.129 0.420 -0.008 -0.059 -0.004 46  PRO   BBB N   
2389 C  CA  . PRO   B 47  ? 0.405 0.051 0.440 -0.060 -0.069 -0.024 46  PRO   BBB CA  
2390 C  C   . PRO   B 47  ? 0.382 0.008 0.469 0.019  -0.025 0.013  46  PRO   BBB C   
2391 O  O   . PRO   B 47  ? 0.394 0.060 0.510 -0.015 -0.010 0.048  46  PRO   BBB O   
2392 C  CB  . PRO   B 47  ? 0.442 0.063 0.462 -0.022 -0.036 0.004  46  PRO   BBB CB  
2393 C  CG  . PRO   B 47  ? 0.437 0.134 0.486 -0.048 -0.070 -0.004 46  PRO   BBB CG  
2394 C  CD  . PRO   B 47  ? 0.465 0.168 0.506 -0.016 -0.118 -0.034 46  PRO   BBB CD  
2395 N  N   . ILE   B 48  ? 0.424 0.008 0.482 -0.023 -0.041 -0.007 47  ILE   BBB N   
2396 C  CA  . ILE   B 48  ? 0.583 0.016 0.471 -0.025 -0.040 0.065  47  ILE   BBB CA  
2397 C  C   . ILE   B 48  ? 0.504 0.010 0.437 0.018  -0.068 0.035  47  ILE   BBB C   
2398 O  O   . ILE   B 48  ? 0.565 0.059 0.508 0.001  -0.053 -0.032 47  ILE   BBB O   
2399 C  CB  . ILE   B 48  ? 0.759 0.172 0.466 0.008  -0.145 -0.088 47  ILE   BBB CB  
2400 C  CG1 . ILE   B 48  ? 1.026 0.017 0.673 -0.020 -0.102 0.082  47  ILE   BBB CG1 
2401 C  CG2 . ILE   B 48  ? 0.728 0.436 0.594 0.107  -0.157 -0.047 47  ILE   BBB CG2 
2402 C  CD1 . ILE   B 48  ? 1.065 0.518 0.679 0.047  -0.127 0.161  47  ILE   BBB CD1 
2403 N  N   . SER   B 49  ? 0.552 0.017 0.480 -0.066 -0.113 0.052  48  SER   BBB N   
2404 C  CA  . SER   B 49  ? 0.666 0.017 0.578 0.008  -0.141 0.072  48  SER   BBB CA  
2405 C  C   . SER   B 49  ? 0.500 0.110 0.539 -0.041 -0.093 -0.008 48  SER   BBB C   
2406 O  O   . SER   B 49  ? 0.495 0.185 0.514 -0.014 -0.068 0.114  48  SER   BBB O   
2407 C  CB  . SER   B 49  ? 0.803 0.144 0.689 -0.177 -0.158 0.050  48  SER   BBB CB  
2408 O  OG  . SER   B 49  ? 0.923 0.105 0.830 -0.104 -0.190 0.058  48  SER   BBB OG  
2409 N  N   . VAL   B 50  ? 0.510 0.024 0.543 -0.046 -0.106 -0.032 49  VAL   BBB N   
2410 C  CA  . VAL   B 50  ? 0.546 0.009 0.534 0.012  -0.070 -0.033 49  VAL   BBB CA  
2411 C  C   . VAL   B 50  ? 0.640 0.029 0.624 0.102  -0.083 0.038  49  VAL   BBB C   
2412 O  O   . VAL   B 50  ? 0.666 0.283 0.546 0.014  -0.000 0.067  49  VAL   BBB O   
2413 C  CB  . VAL   B 50  ? 0.571 0.011 0.549 -0.012 -0.054 0.047  49  VAL   BBB CB  
2414 C  CG1 . VAL   B 50  ? 0.501 0.015 0.696 -0.046 -0.044 0.060  49  VAL   BBB CG1 
2415 C  CG2 . VAL   B 50  ? 0.555 0.019 0.677 -0.006 -0.049 0.009  49  VAL   BBB CG2 
2416 N  N   . SER   B 51  ? 0.666 0.045 0.675 0.112  -0.108 0.094  50  SER   BBB N   
2417 C  CA  A SER   B 51  ? 0.870 0.012 0.852 0.035  0.020  0.064  50  SER   BBB CA  
2418 C  CA  B SER   B 51  ? 0.929 0.011 0.848 0.013  -0.004 0.064  50  SER   BBB CA  
2419 C  C   . SER   B 51  ? 0.834 0.199 0.886 0.071  -0.112 0.007  50  SER   BBB C   
2420 O  O   . SER   B 51  ? 0.947 0.219 0.637 -0.071 -0.007 0.011  50  SER   BBB O   
2421 C  CB  A SER   B 51  ? 0.640 0.233 0.731 0.016  0.019  -0.096 50  SER   BBB CB  
2422 C  CB  B SER   B 51  ? 0.790 0.374 0.700 -0.030 -0.004 -0.022 50  SER   BBB CB  
2423 O  OG  A SER   B 51  ? 0.522 0.089 0.673 -0.078 0.159  0.065  50  SER   BBB OG  
2424 O  OG  B SER   B 51  ? 0.802 0.359 0.486 -0.032 0.100  0.051  50  SER   BBB OG  
2425 N  N   A TYR   B 52  ? 0.873 0.018 0.592 -0.037 -0.086 0.031  51  TYR   BBB N   
2426 N  N   B TYR   B 52  ? 0.828 0.022 0.552 0.061  -0.056 -0.013 51  TYR   BBB N   
2427 C  CA  A TYR   B 52  ? 0.707 0.094 0.567 -0.019 0.049  0.056  51  TYR   BBB CA  
2428 C  CA  B TYR   B 52  ? 0.611 0.019 0.580 -0.067 -0.008 0.057  51  TYR   BBB CA  
2429 C  C   A TYR   B 52  ? 0.737 0.140 0.383 0.009  0.055  0.011  51  TYR   BBB C   
2430 C  C   B TYR   B 52  ? 0.621 0.009 0.339 -0.031 -0.036 -0.015 51  TYR   BBB C   
2431 O  O   A TYR   B 52  ? 0.633 0.032 0.507 -0.039 0.036  0.105  51  TYR   BBB O   
2432 O  O   B TYR   B 52  ? 0.551 0.012 0.490 -0.053 -0.016 -0.013 51  TYR   BBB O   
2433 C  CB  A TYR   B 52  ? 0.639 0.019 0.473 0.074  0.115  -0.028 51  TYR   BBB CB  
2434 C  CB  B TYR   B 52  ? 0.595 0.010 0.513 -0.005 0.076  -0.043 51  TYR   BBB CB  
2435 C  CG  A TYR   B 52  ? 0.500 0.016 0.478 0.064  0.111  0.041  51  TYR   BBB CG  
2436 C  CG  B TYR   B 52  ? 0.339 0.015 0.468 0.053  0.115  0.026  51  TYR   BBB CG  
2437 C  CD1 A TYR   B 52  ? 0.474 0.007 0.426 0.012  0.062  0.020  51  TYR   BBB CD1 
2438 C  CD1 B TYR   B 52  ? 0.311 0.014 0.395 0.021  0.083  0.054  51  TYR   BBB CD1 
2439 C  CD2 A TYR   B 52  ? 0.569 0.013 0.475 -0.001 0.067  0.055  51  TYR   BBB CD2 
2440 C  CD2 B TYR   B 52  ? 0.395 0.011 0.490 0.019  0.097  0.044  51  TYR   BBB CD2 
2441 C  CE1 A TYR   B 52  ? 0.489 0.014 0.418 -0.010 0.138  0.050  51  TYR   BBB CE1 
2442 C  CE1 B TYR   B 52  ? 0.328 0.010 0.388 0.012  0.057  0.038  51  TYR   BBB CE1 
2443 C  CE2 A TYR   B 52  ? 0.474 0.007 0.464 -0.022 0.064  0.003  51  TYR   BBB CE2 
2444 C  CE2 B TYR   B 52  ? 0.384 0.008 0.501 -0.016 0.076  -0.026 51  TYR   BBB CE2 
2445 C  CZ  A TYR   B 52  ? 0.455 0.013 0.440 -0.021 0.054  0.048  51  TYR   BBB CZ  
2446 C  CZ  B TYR   B 52  ? 0.377 0.018 0.411 -0.016 0.040  0.064  51  TYR   BBB CZ  
2447 O  OH  A TYR   B 52  ? 0.361 0.026 0.506 -0.083 0.029  0.004  51  TYR   BBB OH  
2448 O  OH  B TYR   B 52  ? 0.388 0.024 0.458 -0.081 0.034  0.013  51  TYR   BBB OH  
2449 N  N   . ASN   B 53  ? 0.643 0.091 0.389 -0.111 -0.015 0.001  52  ASN   BBB N   
2450 C  CA  . ASN   B 53  ? 0.588 0.119 0.550 0.057  -0.018 0.023  52  ASN   BBB CA  
2451 C  C   . ASN   B 53  ? 0.536 0.292 0.472 -0.079 0.067  0.130  52  ASN   BBB C   
2452 O  O   . ASN   B 53  ? 0.664 0.166 0.456 0.037  -0.031 -0.061 52  ASN   BBB O   
2453 C  CB  . ASN   B 53  ? 0.655 0.098 0.510 -0.012 -0.010 0.051  52  ASN   BBB CB  
2454 C  CG  . ASN   B 53  ? 0.539 0.088 0.481 -0.001 -0.123 0.013  52  ASN   BBB CG  
2455 O  OD1 . ASN   B 53  ? 0.452 0.085 0.507 -0.057 -0.074 0.124  52  ASN   BBB OD1 
2456 N  ND2 . ASN   B 53  ? 0.733 0.377 0.729 -0.250 -0.122 -0.086 52  ASN   BBB ND2 
2457 N  N   . PRO   B 54  ? 0.596 0.163 0.430 -0.047 0.073  0.027  53  PRO   BBB N   
2458 C  CA  . PRO   B 54  ? 0.810 0.048 0.501 -0.184 -0.011 0.009  53  PRO   BBB CA  
2459 C  C   . PRO   B 54  ? 0.693 0.225 0.475 -0.075 -0.054 0.027  53  PRO   BBB C   
2460 O  O   . PRO   B 54  ? 0.693 0.056 0.490 -0.074 -0.042 0.057  53  PRO   BBB O   
2461 C  CB  . PRO   B 54  ? 0.883 0.024 0.679 -0.122 -0.037 -0.016 53  PRO   BBB CB  
2462 C  CG  . PRO   B 54  ? 0.715 0.038 0.590 -0.128 0.031  -0.078 53  PRO   BBB CG  
2463 C  CD  . PRO   B 54  ? 0.771 0.072 0.534 -0.126 -0.003 -0.093 53  PRO   BBB CD  
2464 N  N   . ALA   B 55  ? 0.864 0.021 0.522 -0.063 0.086  -0.080 54  ALA   BBB N   
2465 C  CA  . ALA   B 55  ? 0.646 0.026 0.589 -0.104 0.057  -0.038 54  ALA   BBB CA  
2466 C  C   . ALA   B 55  ? 0.557 0.128 0.363 0.048  -0.019 -0.029 54  ALA   BBB C   
2467 O  O   . ALA   B 55  ? 0.617 0.028 0.411 -0.081 0.015  0.006  54  ALA   BBB O   
2468 C  CB  . ALA   B 55  ? 0.654 0.029 0.529 -0.120 0.047  0.010  54  ALA   BBB CB  
2469 N  N   . THR   B 56  ? 0.604 0.035 0.416 -0.053 -0.005 0.000  55  THR   BBB N   
2470 C  CA  . THR   B 56  ? 0.480 0.160 0.420 -0.051 -0.037 -0.088 55  THR   BBB CA  
2471 C  C   . THR   B 56  ? 0.447 0.185 0.303 -0.045 -0.023 -0.019 55  THR   BBB C   
2472 O  O   . THR   B 56  ? 0.503 0.033 0.389 -0.038 -0.024 0.004  55  THR   BBB O   
2473 C  CB  . THR   B 56  ? 0.472 0.175 0.414 -0.052 -0.072 -0.102 55  THR   BBB CB  
2474 O  OG1 . THR   B 56  ? 0.640 0.097 0.406 -0.102 -0.044 0.005  55  THR   BBB OG1 
2475 C  CG2 . THR   B 56  ? 0.415 0.173 0.460 -0.040 -0.043 -0.081 55  THR   BBB CG2 
2476 N  N   . ALA   B 57  ? 0.456 0.010 0.402 -0.040 -0.020 0.000  56  ALA   BBB N   
2477 C  CA  . ALA   B 57  ? 0.509 0.008 0.375 -0.031 -0.016 -0.008 56  ALA   BBB CA  
2478 C  C   . ALA   B 57  ? 0.502 0.027 0.412 -0.063 0.009  0.071  56  ALA   BBB C   
2479 O  O   . ALA   B 57  ? 0.548 0.011 0.390 -0.030 -0.033 0.035  56  ALA   BBB O   
2480 C  CB  . ALA   B 57  ? 0.545 0.026 0.432 0.104  0.024  0.010  56  ALA   BBB CB  
2481 N  N   . LYS   B 58  ? 0.429 0.010 0.454 0.017  -0.029 0.037  57  LYS   BBB N   
2482 C  CA  . LYS   B 58  ? 0.400 0.015 0.459 -0.058 -0.028 0.013  57  LYS   BBB CA  
2483 C  C   . LYS   B 58  ? 0.356 0.009 0.396 -0.023 0.002  0.018  57  LYS   BBB C   
2484 O  O   . LYS   B 58  ? 0.446 0.041 0.374 0.041  -0.029 -0.001 57  LYS   BBB O   
2485 C  CB  . LYS   B 58  ? 0.441 0.031 0.555 -0.101 0.014  -0.032 57  LYS   BBB CB  
2486 C  CG  . LYS   B 58  ? 0.500 0.112 0.522 -0.120 0.037  -0.050 57  LYS   BBB CG  
2487 C  CD  . LYS   B 58  ? 0.550 0.434 0.625 -0.000 0.041  -0.172 57  LYS   BBB CD  
2488 C  CE  . LYS   B 58  ? 0.773 0.594 0.691 0.049  0.118  -0.233 57  LYS   BBB CE  
2489 N  NZ  . LYS   B 58  ? 1.037 0.480 0.886 0.029  0.117  -0.193 57  LYS   BBB NZ  
2490 N  N   . GLU   B 59  ? 0.337 0.011 0.391 0.019  -0.010 0.036  58  GLU   BBB N   
2491 C  CA  . GLU   B 59  ? 0.344 0.029 0.372 0.033  -0.011 0.037  58  GLU   BBB CA  
2492 C  C   . GLU   B 59  ? 0.339 0.027 0.324 -0.008 -0.046 -0.024 58  GLU   BBB C   
2493 O  O   . GLU   B 59  ? 0.362 0.024 0.377 -0.043 -0.052 0.026  58  GLU   BBB O   
2494 C  CB  . GLU   B 59  ? 0.369 0.115 0.350 0.011  -0.003 -0.022 58  GLU   BBB CB  
2495 C  CG  . GLU   B 59  ? 0.382 0.123 0.416 0.056  -0.009 -0.052 58  GLU   BBB CG  
2496 C  CD  . GLU   B 59  ? 0.453 0.171 0.419 0.095  0.047  -0.053 58  GLU   BBB CD  
2497 O  OE1 . GLU   B 59  ? 0.401 0.143 0.640 0.076  0.093  -0.016 58  GLU   BBB OE1 
2498 O  OE2 . GLU   B 59  ? 0.710 0.170 0.522 0.211  0.053  0.047  58  GLU   BBB OE2 
2499 N  N   . ILE   B 60  ? 0.312 0.014 0.371 -0.041 -0.021 0.028  59  ILE   BBB N   
2500 C  CA  . ILE   B 60  ? 0.276 0.013 0.370 -0.033 -0.011 0.033  59  ILE   BBB CA  
2501 C  C   . ILE   B 60  ? 0.339 0.122 0.328 0.009  -0.012 0.012  59  ILE   BBB C   
2502 O  O   . ILE   B 60  ? 0.355 0.010 0.387 0.037  -0.013 -0.013 59  ILE   BBB O   
2503 C  CB  . ILE   B 60  ? 0.291 0.018 0.385 -0.054 -0.002 0.026  59  ILE   BBB CB  
2504 C  CG1 . ILE   B 60  ? 0.330 0.009 0.465 -0.028 -0.011 -0.004 59  ILE   BBB CG1 
2505 C  CG2 . ILE   B 60  ? 0.305 0.012 0.419 0.035  0.012  0.029  59  ILE   BBB CG2 
2506 C  CD1 . ILE   B 60  ? 0.355 0.030 0.454 -0.036 0.018  0.073  59  ILE   BBB CD1 
2507 N  N   . ILE   B 61  ? 0.334 0.120 0.358 0.006  0.004  0.019  60  ILE   BBB N   
2508 C  CA  . ILE   B 61  ? 0.292 0.031 0.344 -0.024 0.023  0.047  60  ILE   BBB CA  
2509 C  C   . ILE   B 61  ? 0.268 0.035 0.320 -0.046 0.011  0.004  60  ILE   BBB C   
2510 O  O   . ILE   B 61  ? 0.324 0.008 0.383 -0.020 0.004  0.006  60  ILE   BBB O   
2511 C  CB  . ILE   B 61  ? 0.319 0.052 0.353 -0.020 0.041  0.021  60  ILE   BBB CB  
2512 C  CG1 . ILE   B 61  ? 0.308 0.058 0.411 -0.009 0.042  -0.025 60  ILE   BBB CG1 
2513 C  CG2 . ILE   B 61  ? 0.305 0.111 0.400 0.039  0.023  0.018  60  ILE   BBB CG2 
2514 C  CD1 . ILE   B 61  ? 0.318 0.088 0.524 0.012  0.070  -0.050 60  ILE   BBB CD1 
2515 N  N   . ASN   B 62  ? 0.290 0.009 0.357 -0.011 -0.019 0.031  61  ASN   BBB N   
2516 C  CA  . ASN   B 62  ? 0.254 0.008 0.385 -0.022 0.010  0.003  61  ASN   BBB CA  
2517 C  C   . ASN   B 62  ? 0.258 0.031 0.363 -0.012 -0.010 -0.028 61  ASN   BBB C   
2518 O  O   . ASN   B 62  ? 0.318 0.008 0.417 0.020  -0.011 -0.006 61  ASN   BBB O   
2519 C  CB  . ASN   B 62  ? 0.271 0.061 0.410 0.028  -0.016 -0.025 61  ASN   BBB CB  
2520 C  CG  . ASN   B 62  ? 0.240 0.055 0.396 0.044  0.018  -0.027 61  ASN   BBB CG  
2521 O  OD1 . ASN   B 62  ? 0.270 0.012 0.440 0.027  0.007  -0.034 61  ASN   BBB OD1 
2522 N  ND2 . ASN   B 62  ? 0.251 0.039 0.421 0.025  0.006  -0.005 61  ASN   BBB ND2 
2523 N  N   . VAL   B 63  ? 0.270 0.081 0.361 0.003  0.003  -0.005 62  VAL   BBB N   
2524 C  CA  . VAL   B 63  ? 0.255 0.105 0.411 -0.002 -0.004 -0.041 62  VAL   BBB CA  
2525 C  C   . VAL   B 63  ? 0.241 0.085 0.395 0.029  -0.003 -0.014 62  VAL   BBB C   
2526 O  O   . VAL   B 63  ? 0.311 0.012 0.545 0.002  -0.030 -0.055 62  VAL   BBB O   
2527 C  CB  . VAL   B 63  ? 0.297 0.013 0.420 0.014  -0.007 -0.050 62  VAL   BBB CB  
2528 C  CG1 . VAL   B 63  ? 0.324 0.052 0.458 -0.063 -0.042 -0.044 62  VAL   BBB CG1 
2529 C  CG2 . VAL   B 63  ? 0.341 0.014 0.432 0.047  -0.012 -0.026 62  VAL   BBB CG2 
2530 N  N   . GLY   B 64  ? 0.228 0.058 0.408 0.044  -0.008 -0.011 63  GLY   BBB N   
2531 C  CA  . GLY   B 64  ? 0.326 0.124 0.392 -0.017 0.003  -0.062 63  GLY   BBB CA  
2532 C  C   . GLY   B 64  ? 0.317 0.043 0.377 0.008  -0.036 -0.056 63  GLY   BBB C   
2533 O  O   . GLY   B 64  ? 0.337 0.070 0.485 -0.005 -0.043 -0.058 63  GLY   BBB O   
2534 N  N   . HIS   B 65  ? 0.322 0.009 0.381 -0.017 -0.024 -0.021 64  HIS   BBB N   
2535 C  CA  . HIS   B 65  ? 0.355 0.038 0.378 0.011  0.003  -0.009 64  HIS   BBB CA  
2536 C  C   . HIS   B 65  ? 0.340 0.010 0.399 -0.027 0.019  -0.023 64  HIS   BBB C   
2537 O  O   . HIS   B 65  ? 0.471 0.007 0.418 0.007  0.011  -0.018 64  HIS   BBB O   
2538 C  CB  . HIS   B 65  ? 0.333 0.013 0.446 0.010  -0.007 -0.052 64  HIS   BBB CB  
2539 C  CG  . HIS   B 65  ? 0.290 0.036 0.386 0.040  -0.028 0.013  64  HIS   BBB CG  
2540 N  ND1 . HIS   B 65  ? 0.290 0.134 0.513 0.058  0.009  0.018  64  HIS   BBB ND1 
2541 C  CD2 . HIS   B 65  ? 0.309 0.013 0.390 0.028  -0.019 -0.014 64  HIS   BBB CD2 
2542 C  CE1 . HIS   B 65  ? 0.292 0.056 0.461 0.027  0.020  0.058  64  HIS   BBB CE1 
2543 N  NE2 . HIS   B 65  ? 0.329 0.063 0.517 0.022  0.016  0.029  64  HIS   BBB NE2 
2544 N  N   . SER   B 66  ? 0.318 0.018 0.363 -0.047 -0.002 -0.009 65  SER   BBB N   
2545 C  CA  . SER   B 66  ? 0.316 0.054 0.348 -0.001 0.004  -0.001 65  SER   BBB CA  
2546 C  C   . SER   B 66  ? 0.304 0.051 0.316 0.008  -0.036 -0.018 65  SER   BBB C   
2547 O  O   . SER   B 66  ? 0.315 0.007 0.372 -0.006 0.005  -0.012 65  SER   BBB O   
2548 C  CB  . SER   B 66  ? 0.344 0.102 0.333 0.000  -0.011 0.004  65  SER   BBB CB  
2549 O  OG  . SER   B 66  ? 0.389 0.007 0.389 0.017  -0.027 0.005  65  SER   BBB OG  
2550 N  N   . PHE   B 67  ? 0.298 0.015 0.337 -0.046 0.014  -0.012 66  PHE   BBB N   
2551 C  CA  . PHE   B 67  ? 0.268 0.042 0.362 -0.037 -0.015 0.042  66  PHE   BBB CA  
2552 C  C   . PHE   B 67  ? 0.284 0.033 0.329 -0.008 0.012  -0.037 66  PHE   BBB C   
2553 O  O   . PHE   B 67  ? 0.332 0.009 0.372 -0.026 -0.015 0.005  66  PHE   BBB O   
2554 C  CB  . PHE   B 67  ? 0.294 0.013 0.338 -0.016 -0.015 -0.009 66  PHE   BBB CB  
2555 C  CG  . PHE   B 67  ? 0.268 0.044 0.345 -0.027 -0.016 -0.021 66  PHE   BBB CG  
2556 C  CD1 . PHE   B 67  ? 0.303 0.042 0.377 -0.000 0.008  0.024  66  PHE   BBB CD1 
2557 C  CD2 . PHE   B 67  ? 0.323 0.007 0.364 -0.005 -0.010 0.011  66  PHE   BBB CD2 
2558 C  CE1 . PHE   B 67  ? 0.305 0.015 0.379 0.020  -0.008 -0.044 66  PHE   BBB CE1 
2559 C  CE2 . PHE   B 67  ? 0.326 0.044 0.390 0.105  0.011  0.006  66  PHE   BBB CE2 
2560 C  CZ  . PHE   B 67  ? 0.351 0.017 0.441 0.054  0.002  -0.034 66  PHE   BBB CZ  
2561 N  N   . HIS   B 68  ? 0.269 0.008 0.359 0.018  -0.007 0.012  67  HIS   BBB N   
2562 C  CA  . HIS   B 68  ? 0.255 0.008 0.408 0.008  -0.031 0.026  67  HIS   BBB CA  
2563 C  C   . HIS   B 68  ? 0.277 0.009 0.339 0.026  -0.025 0.005  67  HIS   BBB C   
2564 O  O   . HIS   B 68  ? 0.350 0.008 0.387 0.022  -0.025 -0.015 67  HIS   BBB O   
2565 C  CB  . HIS   B 68  ? 0.275 0.008 0.380 0.000  -0.031 -0.023 67  HIS   BBB CB  
2566 C  CG  . HIS   B 68  ? 0.280 0.006 0.408 0.002  0.015  0.001  67  HIS   BBB CG  
2567 N  ND1 . HIS   B 68  ? 0.302 0.007 0.412 0.006  0.018  0.006  67  HIS   BBB ND1 
2568 C  CD2 . HIS   B 68  ? 0.280 0.012 0.414 0.030  -0.000 -0.028 67  HIS   BBB CD2 
2569 C  CE1 . HIS   B 68  ? 0.292 0.007 0.463 -0.002 0.014  -0.018 67  HIS   BBB CE1 
2570 N  NE2 . HIS   B 68  ? 0.285 0.013 0.509 0.033  0.048  -0.031 67  HIS   BBB NE2 
2571 N  N   . VAL   B 69  ? 0.305 0.016 0.336 -0.041 -0.014 0.039  68  VAL   BBB N   
2572 C  CA  . VAL   B 69  ? 0.328 0.025 0.364 -0.071 -0.017 0.037  68  VAL   BBB CA  
2573 C  C   . VAL   B 69  ? 0.337 0.011 0.326 -0.040 -0.025 -0.001 68  VAL   BBB C   
2574 O  O   . VAL   B 69  ? 0.355 0.016 0.358 -0.042 -0.006 0.040  68  VAL   BBB O   
2575 C  CB  . VAL   B 69  ? 0.326 0.015 0.392 -0.035 -0.016 0.046  68  VAL   BBB CB  
2576 C  CG1 . VAL   B 69  ? 0.353 0.007 0.437 -0.006 -0.085 0.010  68  VAL   BBB CG1 
2577 C  CG2 . VAL   B 69  ? 0.327 0.052 0.397 0.006  -0.041 0.004  68  VAL   BBB CG2 
2578 N  N   . ASN   B 70  ? 0.314 0.011 0.344 0.029  0.006  0.024  69  ASN   BBB N   
2579 C  CA  . ASN   B 70  ? 0.323 0.019 0.397 -0.052 -0.017 0.041  69  ASN   BBB CA  
2580 C  C   . ASN   B 70  ? 0.253 0.019 0.383 -0.034 -0.036 0.017  69  ASN   BBB C   
2581 O  O   . ASN   B 70  ? 0.295 0.025 0.415 -0.012 -0.048 0.016  69  ASN   BBB O   
2582 C  CB  . ASN   B 70  ? 0.311 0.020 0.431 -0.065 -0.004 -0.007 69  ASN   BBB CB  
2583 C  CG  . ASN   B 70  ? 0.293 0.014 0.377 -0.047 -0.043 0.002  69  ASN   BBB CG  
2584 O  OD1 . ASN   B 70  ? 0.437 0.011 0.524 0.023  -0.002 0.042  69  ASN   BBB OD1 
2585 N  ND2 . ASN   B 70  ? 0.334 0.016 0.410 -0.002 -0.033 -0.020 69  ASN   BBB ND2 
2586 N  N   . PHE   B 71  ? 0.307 0.015 0.405 -0.051 -0.057 -0.001 70  PHE   BBB N   
2587 C  CA  . PHE   B 71  ? 0.449 0.026 0.454 -0.088 -0.070 0.043  70  PHE   BBB CA  
2588 C  C   . PHE   B 71  ? 0.440 0.023 0.457 -0.047 -0.018 0.074  70  PHE   BBB C   
2589 O  O   . PHE   B 71  ? 0.384 0.061 0.494 -0.104 -0.008 0.021  70  PHE   BBB O   
2590 C  CB  . PHE   B 71  ? 0.469 0.016 0.473 -0.065 -0.033 0.008  70  PHE   BBB CB  
2591 C  CG  . PHE   B 71  ? 0.473 0.047 0.396 -0.137 0.006  -0.002 70  PHE   BBB CG  
2592 C  CD1 . PHE   B 71  ? 0.459 0.032 0.386 -0.106 -0.013 0.022  70  PHE   BBB CD1 
2593 C  CD2 . PHE   B 71  ? 0.461 0.036 0.365 -0.075 -0.053 0.038  70  PHE   BBB CD2 
2594 C  CE1 . PHE   B 71  ? 0.480 0.094 0.350 -0.050 -0.000 -0.003 70  PHE   BBB CE1 
2595 C  CE2 . PHE   B 71  ? 0.492 0.020 0.411 -0.080 -0.020 -0.010 70  PHE   BBB CE2 
2596 C  CZ  . PHE   B 71  ? 0.444 0.053 0.383 -0.143 0.018  -0.001 70  PHE   BBB CZ  
2597 N  N   . GLU   B 72  ? 0.408 0.038 0.413 -0.093 -0.082 0.083  71  GLU   BBB N   
2598 C  CA  . GLU   B 72  ? 0.425 0.077 0.527 -0.115 -0.059 0.038  71  GLU   BBB CA  
2599 C  C   . GLU   B 72  ? 0.514 0.142 0.522 -0.139 -0.070 0.108  71  GLU   BBB C   
2600 O  O   . GLU   B 72  ? 0.679 0.262 0.476 -0.179 -0.089 0.159  71  GLU   BBB O   
2601 C  CB  . GLU   B 72  ? 0.489 0.073 0.537 -0.108 -0.027 0.061  71  GLU   BBB CB  
2602 C  CG  . GLU   B 72  ? 0.583 0.252 0.621 -0.091 -0.064 0.098  71  GLU   BBB CG  
2603 C  CD  . GLU   B 72  ? 0.910 0.275 0.746 -0.106 -0.167 0.133  71  GLU   BBB CD  
2604 O  OE1 . GLU   B 72  ? 0.919 0.416 0.957 -0.114 -0.284 0.000  71  GLU   BBB OE1 
2605 O  OE2 . GLU   B 72  ? 0.949 0.514 0.904 -0.086 -0.213 0.203  71  GLU   BBB OE2 
2606 N  N   . ASP   B 73  ? 0.550 0.198 0.577 -0.165 -0.036 0.137  72  ASP   BBB N   
2607 C  CA  . ASP   B 73  ? 0.563 0.276 0.711 -0.150 -0.080 0.161  72  ASP   BBB CA  
2608 C  C   . ASP   B 73  ? 0.589 0.509 0.805 -0.197 0.004  0.235  72  ASP   BBB C   
2609 O  O   . ASP   B 73  ? 0.718 0.469 0.659 -0.173 -0.110 0.037  72  ASP   BBB O   
2610 C  CB  . ASP   B 73  ? 0.532 0.280 0.618 -0.211 -0.073 0.174  72  ASP   BBB CB  
2611 C  CG  . ASP   B 73  ? 0.581 0.403 0.541 -0.237 -0.174 0.070  72  ASP   BBB CG  
2612 O  OD1 . ASP   B 73  ? 0.561 0.312 0.586 -0.055 -0.130 0.111  72  ASP   BBB OD1 
2613 O  OD2 . ASP   B 73  ? 0.537 0.521 0.850 0.030  -0.107 0.240  72  ASP   BBB OD2 
2614 N  N   . ASN   B 74  ? 0.468 0.325 0.855 -0.186 -0.108 0.117  73  ASN   BBB N   
2615 C  CA  . ASN   B 74  ? 0.432 0.473 0.886 -0.132 -0.075 0.064  73  ASN   BBB CA  
2616 C  C   . ASN   B 74  ? 0.544 0.438 0.743 -0.101 -0.011 0.086  73  ASN   BBB C   
2617 O  O   . ASN   B 74  ? 0.561 0.405 0.780 -0.228 -0.039 0.010  73  ASN   BBB O   
2618 C  CB  . ASN   B 74  ? 0.606 0.568 1.002 -0.150 -0.155 0.162  73  ASN   BBB CB  
2619 C  CG  . ASN   B 74  ? 0.888 0.623 1.363 -0.096 -0.470 -0.128 73  ASN   BBB CG  
2620 O  OD1 . ASN   B 74  ? 0.885 0.756 1.402 -0.101 -0.375 0.445  73  ASN   BBB OD1 
2621 N  ND2 . ASN   B 74  ? 1.062 1.117 1.496 -0.106 -0.146 0.338  73  ASN   BBB ND2 
2622 N  N   . ASP   B 75  ? 0.559 0.215 0.674 -0.163 -0.051 0.010  74  ASP   BBB N   
2623 C  CA  . ASP   B 75  ? 0.578 0.135 0.672 -0.141 -0.080 0.081  74  ASP   BBB CA  
2624 C  C   . ASP   B 75  ? 0.532 0.319 0.606 -0.164 -0.174 0.174  74  ASP   BBB C   
2625 O  O   . ASP   B 75  ? 0.551 0.283 0.734 -0.209 -0.068 0.082  74  ASP   BBB O   
2626 C  CB  . ASP   B 75  ? 0.623 0.235 0.770 -0.241 -0.145 0.205  74  ASP   BBB CB  
2627 C  CG  . ASP   B 75  ? 0.613 0.327 0.721 -0.147 -0.030 0.139  74  ASP   BBB CG  
2628 O  OD1 . ASP   B 75  ? 0.690 0.182 0.566 -0.283 -0.158 0.149  74  ASP   BBB OD1 
2629 O  OD2 . ASP   B 75  ? 0.748 0.534 0.775 -0.265 -0.133 0.350  74  ASP   BBB OD2 
2630 N  N   . ASN   B 76  ? 0.529 0.295 0.561 -0.218 -0.076 0.095  75  ASN   BBB N   
2631 C  CA  . ASN   B 76  ? 0.386 0.267 0.495 -0.011 0.029  -0.012 75  ASN   BBB CA  
2632 C  C   . ASN   B 76  ? 0.342 0.021 0.541 -0.068 -0.066 -0.009 75  ASN   BBB C   
2633 O  O   . ASN   B 76  ? 0.753 0.328 0.479 -0.077 -0.035 0.131  75  ASN   BBB O   
2634 C  CB  . ASN   B 76  ? 0.350 0.302 0.623 -0.035 -0.044 0.004  75  ASN   BBB CB  
2635 C  CG  . ASN   B 76  ? 0.565 0.490 0.715 0.040  -0.030 -0.127 75  ASN   BBB CG  
2636 O  OD1 . ASN   B 76  ? 0.479 0.488 0.903 -0.044 0.003  -0.072 75  ASN   BBB OD1 
2637 N  ND2 . ASN   B 76  ? 0.663 0.645 0.835 -0.057 -0.190 -0.219 75  ASN   BBB ND2 
2638 N  N   . ARG   B 77  ? 0.561 0.127 0.566 -0.119 -0.162 0.115  76  ARG   BBB N   
2639 C  CA  . ARG   B 77  ? 0.626 0.115 0.579 -0.228 -0.093 -0.083 76  ARG   BBB CA  
2640 C  C   . ARG   B 77  ? 0.656 0.137 0.522 -0.147 -0.049 0.066  76  ARG   BBB C   
2641 O  O   . ARG   B 77  ? 0.737 0.113 0.432 -0.141 -0.109 0.036  76  ARG   BBB O   
2642 C  CB  . ARG   B 77  ? 0.681 0.091 0.739 -0.234 -0.143 0.100  76  ARG   BBB CB  
2643 C  CG  . ARG   B 77  ? 0.846 0.083 0.716 -0.225 -0.127 0.141  76  ARG   BBB CG  
2644 C  CD  . ARG   B 77  ? 0.812 0.128 0.694 -0.193 -0.210 0.048  76  ARG   BBB CD  
2645 N  NE  . ARG   B 77  ? 0.615 0.049 0.696 -0.134 -0.125 0.122  76  ARG   BBB NE  
2646 C  CZ  . ARG   B 77  ? 0.627 0.104 0.722 0.070  -0.136 0.027  76  ARG   BBB CZ  
2647 N  NH1 . ARG   B 77  ? 0.622 0.055 0.595 -0.015 -0.073 -0.007 76  ARG   BBB NH1 
2648 N  NH2 . ARG   B 77  ? 0.596 0.328 0.442 -0.214 -0.062 0.125  76  ARG   BBB NH2 
2649 N  N   . SER   B 78  ? 0.544 0.161 0.482 -0.142 -0.061 0.027  77  SER   BBB N   
2650 C  CA  . SER   B 78  ? 0.469 0.197 0.463 -0.052 -0.057 0.096  77  SER   BBB CA  
2651 C  C   . SER   B 78  ? 0.466 0.044 0.481 -0.123 -0.013 0.012  77  SER   BBB C   
2652 O  O   . SER   B 78  ? 0.464 0.033 0.469 -0.048 -0.021 0.079  77  SER   BBB O   
2653 C  CB  . SER   B 78  ? 0.463 0.073 0.479 -0.114 -0.047 0.058  77  SER   BBB CB  
2654 O  OG  . SER   B 78  ? 0.573 0.018 0.520 -0.031 -0.017 -0.071 77  SER   BBB OG  
2655 N  N   . VAL   B 79  ? 0.574 0.031 0.519 -0.106 -0.063 0.042  78  VAL   BBB N   
2656 C  CA  . VAL   B 79  ? 0.593 0.160 0.413 -0.067 -0.134 0.060  78  VAL   BBB CA  
2657 C  C   . VAL   B 79  ? 0.533 0.129 0.473 -0.049 -0.105 0.099  78  VAL   BBB C   
2658 O  O   . VAL   B 79  ? 0.524 0.078 0.465 -0.130 -0.115 0.044  78  VAL   BBB O   
2659 C  CB  . VAL   B 79  ? 0.622 0.190 0.524 -0.105 -0.106 0.122  78  VAL   BBB CB  
2660 C  CG1 . VAL   B 79  ? 0.621 0.376 0.571 -0.209 -0.112 0.120  78  VAL   BBB CG1 
2661 C  CG2 . VAL   B 79  ? 0.874 0.294 0.590 -0.223 -0.045 -0.014 78  VAL   BBB CG2 
2662 N  N   . LEU   B 80  ? 0.475 0.120 0.475 -0.048 -0.114 0.069  79  LEU   BBB N   
2663 C  CA  . LEU   B 80  ? 0.433 0.072 0.474 -0.066 -0.091 0.053  79  LEU   BBB CA  
2664 C  C   . LEU   B 80  ? 0.385 0.046 0.511 -0.105 -0.055 0.085  79  LEU   BBB C   
2665 O  O   . LEU   B 80  ? 0.391 0.154 0.512 -0.035 -0.065 0.060  79  LEU   BBB O   
2666 C  CB  . LEU   B 80  ? 0.443 0.108 0.428 -0.127 -0.130 0.077  79  LEU   BBB CB  
2667 C  CG  . LEU   B 80  ? 0.489 0.034 0.420 -0.069 -0.070 0.039  79  LEU   BBB CG  
2668 C  CD1 . LEU   B 80  ? 0.494 0.035 0.424 -0.005 -0.050 0.012  79  LEU   BBB CD1 
2669 C  CD2 . LEU   B 80  ? 0.505 0.042 0.450 -0.098 -0.066 0.046  79  LEU   BBB CD2 
2670 N  N   . LYS   B 81  ? 0.506 0.035 0.498 -0.058 -0.075 0.111  80  LYS   BBB N   
2671 C  CA  . LYS   B 81  ? 0.520 0.119 0.459 -0.084 -0.092 0.001  80  LYS   BBB CA  
2672 C  C   . LYS   B 81  ? 0.451 0.014 0.413 -0.023 -0.100 -0.010 80  LYS   BBB C   
2673 O  O   . LYS   B 81  ? 0.421 0.113 0.463 -0.071 -0.076 0.090  80  LYS   BBB O   
2674 C  CB  . LYS   B 81  ? 0.546 0.300 0.645 -0.261 -0.178 0.061  80  LYS   BBB CB  
2675 C  CG  . LYS   B 81  ? 0.713 0.248 0.871 -0.306 -0.184 -0.054 80  LYS   BBB CG  
2676 C  CD  . LYS   B 81  ? 0.967 0.237 0.798 -0.411 -0.173 0.045  80  LYS   BBB CD  
2677 C  CE  . LYS   B 81  ? 1.022 0.454 1.101 -0.350 -0.039 -0.040 80  LYS   BBB CE  
2678 N  NZ  . LYS   B 81  ? 1.218 0.155 1.230 -0.166 -0.059 -0.162 80  LYS   BBB NZ  
2679 N  N   . GLY   B 82  ? 0.401 0.215 0.425 -0.082 -0.106 0.037  81  GLY   BBB N   
2680 C  CA  . GLY   B 82  ? 0.470 0.081 0.433 -0.044 -0.076 0.069  81  GLY   BBB CA  
2681 C  C   . GLY   B 82  ? 0.400 0.087 0.399 -0.051 -0.027 0.059  81  GLY   BBB C   
2682 O  O   . GLY   B 82  ? 0.436 0.028 0.423 -0.080 -0.049 0.045  81  GLY   BBB O   
2683 N  N   . GLY   B 83  ? 0.369 0.034 0.445 -0.043 -0.007 0.033  82  GLY   BBB N   
2684 C  CA  . GLY   B 83  ? 0.375 0.058 0.419 -0.095 -0.004 0.077  82  GLY   BBB CA  
2685 C  C   . GLY   B 83  ? 0.394 0.162 0.391 -0.038 -0.058 0.069  82  GLY   BBB C   
2686 O  O   . GLY   B 83  ? 0.387 0.085 0.498 -0.058 -0.108 0.081  82  GLY   BBB O   
2687 N  N   . PRO   B 84  ? 0.369 0.155 0.427 -0.056 -0.020 0.064  83  PRO   BBB N   
2688 C  CA  . PRO   B 84  ? 0.392 0.180 0.456 -0.032 -0.040 0.042  83  PRO   BBB CA  
2689 C  C   . PRO   B 84  ? 0.341 0.228 0.508 0.011  -0.057 0.115  83  PRO   BBB C   
2690 O  O   . PRO   B 84  ? 0.344 0.218 0.642 0.013  -0.011 0.159  83  PRO   BBB O   
2691 C  CB  . PRO   B 84  ? 0.401 0.134 0.508 -0.047 -0.012 0.059  83  PRO   BBB CB  
2692 C  CG  . PRO   B 84  ? 0.412 0.093 0.467 -0.107 -0.038 0.020  83  PRO   BBB CG  
2693 C  CD  . PRO   B 84  ? 0.459 0.091 0.426 -0.073 -0.041 0.024  83  PRO   BBB CD  
2694 N  N   . PHE   B 85  ? 0.375 0.132 0.468 -0.082 -0.052 0.079  84  PHE   BBB N   
2695 C  CA  . PHE   B 85  ? 0.324 0.226 0.494 -0.114 -0.059 0.085  84  PHE   BBB CA  
2696 C  C   . PHE   B 85  ? 0.384 0.316 0.508 -0.125 -0.097 0.031  84  PHE   BBB C   
2697 O  O   . PHE   B 85  ? 0.526 0.211 0.555 -0.195 -0.121 0.018  84  PHE   BBB O   
2698 C  CB  . PHE   B 85  ? 0.404 0.180 0.474 -0.146 -0.081 0.094  84  PHE   BBB CB  
2699 C  CG  . PHE   B 85  ? 0.439 0.139 0.430 -0.126 -0.084 0.062  84  PHE   BBB CG  
2700 C  CD1 . PHE   B 85  ? 0.477 0.250 0.488 -0.184 0.017  -0.023 84  PHE   BBB CD1 
2701 C  CD2 . PHE   B 85  ? 0.430 0.215 0.508 -0.135 -0.093 0.131  84  PHE   BBB CD2 
2702 C  CE1 . PHE   B 85  ? 0.555 0.022 0.566 -0.088 0.023  0.019  84  PHE   BBB CE1 
2703 C  CE2 . PHE   B 85  ? 0.466 0.201 0.448 -0.089 -0.088 0.079  84  PHE   BBB CE2 
2704 C  CZ  . PHE   B 85  ? 0.494 0.179 0.523 -0.130 -0.032 0.058  84  PHE   BBB CZ  
2705 N  N   . SER   B 86  ? 0.395 0.366 0.608 -0.182 -0.081 0.140  85  SER   BBB N   
2706 C  CA  . SER   B 86  ? 0.427 0.409 0.549 -0.227 -0.030 0.128  85  SER   BBB CA  
2707 C  C   . SER   B 86  ? 0.529 0.399 0.589 -0.172 -0.085 0.138  85  SER   BBB C   
2708 O  O   . SER   B 86  ? 0.560 0.428 0.864 -0.250 0.036  0.089  85  SER   BBB O   
2709 C  CB  . SER   B 86  ? 0.438 0.559 0.713 -0.161 -0.062 0.037  85  SER   BBB CB  
2710 O  OG  . SER   B 86  ? 0.456 0.671 0.835 -0.019 0.038  0.042  85  SER   BBB OG  
2711 N  N   . ASP   B 87  ? 0.461 0.651 0.579 -0.239 -0.118 0.181  86  ASP   BBB N   
2712 C  CA  . ASP   B 87  ? 0.434 0.663 0.644 -0.194 -0.100 0.228  86  ASP   BBB CA  
2713 C  C   . ASP   B 87  ? 0.494 0.341 0.626 -0.163 -0.096 0.222  86  ASP   BBB C   
2714 O  O   . ASP   B 87  ? 0.471 0.345 0.668 -0.106 -0.048 0.222  86  ASP   BBB O   
2715 C  CB  . ASP   B 87  ? 0.486 0.723 0.690 -0.121 0.015  0.240  86  ASP   BBB CB  
2716 C  CG  . ASP   B 87  ? 0.500 0.759 0.870 -0.109 -0.188 0.195  86  ASP   BBB CG  
2717 O  OD1 . ASP   B 87  ? 0.601 0.656 0.896 -0.231 -0.130 0.187  86  ASP   BBB OD1 
2718 O  OD2 . ASP   B 87  ? 0.823 0.750 0.811 -0.357 -0.179 0.228  86  ASP   BBB OD2 
2719 N  N   . SER   B 88  ? 0.537 0.267 0.691 -0.136 -0.175 0.191  87  SER   BBB N   
2720 C  CA  . SER   B 88  ? 0.573 0.304 0.668 -0.136 -0.199 0.098  87  SER   BBB CA  
2721 C  C   . SER   B 88  ? 0.337 0.153 0.679 -0.053 -0.096 0.143  87  SER   BBB C   
2722 O  O   . SER   B 88  ? 0.403 0.185 0.671 -0.056 -0.075 0.105  87  SER   BBB O   
2723 C  CB  . SER   B 88  ? 0.632 0.355 0.691 -0.156 -0.201 0.161  87  SER   BBB CB  
2724 O  OG  . SER   B 88  ? 0.680 0.428 0.752 -0.203 -0.267 0.109  87  SER   BBB OG  
2725 N  N   . TYR   B 89  ? 0.375 0.194 0.529 -0.120 -0.130 0.123  88  TYR   BBB N   
2726 C  CA  . TYR   B 89  ? 0.382 0.204 0.505 -0.155 -0.120 0.158  88  TYR   BBB CA  
2727 C  C   . TYR   B 89  ? 0.471 0.073 0.476 -0.110 -0.112 0.090  88  TYR   BBB C   
2728 O  O   . TYR   B 89  ? 0.424 0.127 0.499 -0.077 -0.089 0.127  88  TYR   BBB O   
2729 C  CB  . TYR   B 89  ? 0.330 0.186 0.536 -0.154 -0.080 0.084  88  TYR   BBB CB  
2730 C  CG  . TYR   B 89  ? 0.387 0.203 0.479 -0.141 -0.062 0.138  88  TYR   BBB CG  
2731 C  CD1 . TYR   B 89  ? 0.369 0.231 0.553 -0.084 -0.112 0.158  88  TYR   BBB CD1 
2732 C  CD2 . TYR   B 89  ? 0.424 0.155 0.492 -0.050 -0.110 0.161  88  TYR   BBB CD2 
2733 C  CE1 . TYR   B 89  ? 0.377 0.265 0.492 -0.087 -0.136 0.192  88  TYR   BBB CE1 
2734 C  CE2 . TYR   B 89  ? 0.424 0.069 0.544 -0.153 -0.116 0.097  88  TYR   BBB CE2 
2735 C  CZ  . TYR   B 89  ? 0.367 0.329 0.485 -0.079 -0.084 0.166  88  TYR   BBB CZ  
2736 O  OH  . TYR   B 89  ? 0.368 0.360 0.615 -0.023 -0.066 0.162  88  TYR   BBB OH  
2737 N  N   . ARG   B 90  ? 0.503 0.136 0.461 -0.206 -0.155 0.102  89  ARG   BBB N   
2738 C  CA  . ARG   B 90  ? 0.429 0.242 0.437 -0.144 -0.135 0.106  89  ARG   BBB CA  
2739 C  C   . ARG   B 90  ? 0.381 0.178 0.409 -0.093 -0.077 0.064  89  ARG   BBB C   
2740 O  O   . ARG   B 90  ? 0.360 0.156 0.460 -0.039 -0.057 0.069  89  ARG   BBB O   
2741 C  CB  . ARG   B 90  ? 0.386 0.358 0.548 -0.131 -0.078 0.150  89  ARG   BBB CB  
2742 C  CG  . ARG   B 90  ? 0.417 0.349 0.576 -0.073 -0.055 0.137  89  ARG   BBB CG  
2743 C  CD  . ARG   B 90  ? 0.613 0.288 0.621 -0.102 0.039  0.168  89  ARG   BBB CD  
2744 N  NE  . ARG   B 90  ? 0.673 0.463 0.734 -0.087 -0.052 0.142  89  ARG   BBB NE  
2745 C  CZ  . ARG   B 90  ? 0.638 0.327 0.676 -0.082 -0.042 -0.067 89  ARG   BBB CZ  
2746 N  NH1 . ARG   B 90  ? 0.649 0.291 0.668 -0.011 0.093  0.091  89  ARG   BBB NH1 
2747 N  NH2 . ARG   B 90  ? 0.792 0.710 0.849 -0.232 -0.116 -0.046 89  ARG   BBB NH2 
2748 N  N   . LEU   B 91  ? 0.389 0.112 0.429 -0.070 -0.071 0.111  90  LEU   BBB N   
2749 C  CA  . LEU   B 91  ? 0.453 0.020 0.426 -0.077 -0.082 0.027  90  LEU   BBB CA  
2750 C  C   . LEU   B 91  ? 0.368 0.041 0.396 -0.111 -0.067 0.037  90  LEU   BBB C   
2751 O  O   . LEU   B 91  ? 0.432 0.034 0.394 -0.070 -0.057 0.087  90  LEU   BBB O   
2752 C  CB  . LEU   B 91  ? 0.427 0.029 0.427 -0.071 -0.023 0.073  90  LEU   BBB CB  
2753 C  CG  . LEU   B 91  ? 0.465 0.056 0.458 -0.138 -0.032 0.070  90  LEU   BBB CG  
2754 C  CD1 . LEU   B 91  ? 0.485 0.043 0.480 -0.133 -0.008 -0.004 90  LEU   BBB CD1 
2755 C  CD2 . LEU   B 91  ? 0.429 0.168 0.457 -0.071 0.009  -0.037 90  LEU   BBB CD2 
2756 N  N   . PHE   B 92  ? 0.375 0.028 0.423 -0.089 -0.048 0.028  91  PHE   BBB N   
2757 C  CA  . PHE   B 92  ? 0.353 0.025 0.436 -0.078 -0.046 0.033  91  PHE   BBB CA  
2758 C  C   . PHE   B 92  ? 0.312 0.034 0.328 -0.068 0.001  0.008  91  PHE   BBB C   
2759 O  O   . PHE   B 92  ? 0.401 0.016 0.411 -0.059 -0.043 0.029  91  PHE   BBB O   
2760 C  CB  . PHE   B 92  ? 0.347 0.043 0.443 -0.043 -0.029 0.082  91  PHE   BBB CB  
2761 C  CG  . PHE   B 92  ? 0.308 0.039 0.436 -0.044 -0.025 0.060  91  PHE   BBB CG  
2762 C  CD1 . PHE   B 92  ? 0.329 0.038 0.456 -0.028 -0.035 0.042  91  PHE   BBB CD1 
2763 C  CD2 . PHE   B 92  ? 0.284 0.008 0.468 -0.017 -0.029 0.017  91  PHE   BBB CD2 
2764 C  CE1 . PHE   B 92  ? 0.323 0.050 0.467 -0.076 -0.044 0.070  91  PHE   BBB CE1 
2765 C  CE2 . PHE   B 92  ? 0.361 0.040 0.417 -0.108 -0.058 0.038  91  PHE   BBB CE2 
2766 C  CZ  . PHE   B 92  ? 0.333 0.030 0.470 -0.074 -0.046 0.068  91  PHE   BBB CZ  
2767 N  N   . GLN   B 93  ? 0.329 0.023 0.341 -0.031 -0.025 0.069  92  GLN   BBB N   
2768 C  CA  . GLN   B 93  ? 0.332 0.009 0.367 -0.014 -0.038 0.026  92  GLN   BBB CA  
2769 C  C   . GLN   B 93  ? 0.337 0.019 0.350 -0.051 -0.050 -0.034 92  GLN   BBB C   
2770 O  O   . GLN   B 93  ? 0.306 0.023 0.389 -0.071 -0.039 0.000  92  GLN   BBB O   
2771 C  CB  . GLN   B 93  ? 0.351 0.096 0.369 -0.035 -0.003 -0.039 92  GLN   BBB CB  
2772 C  CG  . GLN   B 93  ? 0.348 0.114 0.441 -0.028 -0.015 -0.007 92  GLN   BBB CG  
2773 C  CD  . GLN   B 93  ? 0.342 0.065 0.452 0.001  0.029  0.066  92  GLN   BBB CD  
2774 O  OE1 . GLN   B 93  ? 0.380 0.017 0.439 -0.039 0.011  0.002  92  GLN   BBB OE1 
2775 N  NE2 . GLN   B 93  ? 0.380 0.046 0.484 -0.078 0.052  0.017  92  GLN   BBB NE2 
2776 N  N   . PHE   B 94  ? 0.337 0.011 0.417 -0.023 -0.039 0.036  93  PHE   BBB N   
2777 C  CA  . PHE   B 94  ? 0.300 0.022 0.321 -0.035 -0.038 0.033  93  PHE   BBB CA  
2778 C  C   . PHE   B 94  ? 0.287 0.008 0.346 -0.013 -0.034 0.021  93  PHE   BBB C   
2779 O  O   . PHE   B 94  ? 0.312 0.009 0.379 -0.030 -0.035 0.009  93  PHE   BBB O   
2780 C  CB  . PHE   B 94  ? 0.294 0.051 0.328 -0.009 -0.033 0.042  93  PHE   BBB CB  
2781 C  CG  . PHE   B 94  ? 0.311 0.009 0.370 -0.016 -0.054 0.025  93  PHE   BBB CG  
2782 C  CD1 . PHE   B 94  ? 0.311 0.008 0.459 -0.025 -0.075 0.004  93  PHE   BBB CD1 
2783 C  CD2 . PHE   B 94  ? 0.312 0.011 0.412 -0.034 -0.012 -0.020 93  PHE   BBB CD2 
2784 C  CE1 . PHE   B 94  ? 0.281 0.014 0.408 -0.045 -0.034 0.021  93  PHE   BBB CE1 
2785 C  CE2 . PHE   B 94  ? 0.360 0.011 0.395 0.010  -0.016 -0.026 93  PHE   BBB CE2 
2786 C  CZ  . PHE   B 94  ? 0.382 0.006 0.412 -0.003 -0.083 0.008  93  PHE   BBB CZ  
2787 N  N   . HIS   B 95  ? 0.313 0.018 0.412 -0.030 -0.026 0.061  94  HIS   BBB N   
2788 C  CA  . HIS   B 95  ? 0.262 0.071 0.349 0.012  -0.013 0.028  94  HIS   BBB CA  
2789 C  C   . HIS   B 95  ? 0.261 0.007 0.396 0.008  -0.028 0.018  94  HIS   BBB C   
2790 O  O   . HIS   B 95  ? 0.357 0.008 0.423 -0.022 -0.040 0.017  94  HIS   BBB O   
2791 C  CB  . HIS   B 95  ? 0.264 0.022 0.388 -0.017 -0.016 0.010  94  HIS   BBB CB  
2792 C  CG  . HIS   B 95  ? 0.278 0.007 0.399 -0.010 -0.040 -0.011 94  HIS   BBB CG  
2793 N  ND1 . HIS   B 95  ? 0.269 0.008 0.479 0.021  -0.011 -0.013 94  HIS   BBB ND1 
2794 C  CD2 . HIS   B 95  ? 0.350 0.034 0.404 -0.097 -0.013 -0.004 94  HIS   BBB CD2 
2795 C  CE1 . HIS   B 95  ? 0.290 0.073 0.443 0.098  0.024  0.104  94  HIS   BBB CE1 
2796 N  NE2 . HIS   B 95  ? 0.519 0.008 0.669 0.015  -0.005 0.023  94  HIS   BBB NE2 
2797 N  N   . PHE   B 96  ? 0.225 0.011 0.332 0.009  -0.032 -0.013 95  PHE   BBB N   
2798 C  CA  . PHE   B 96  ? 0.274 0.009 0.322 0.000  0.014  -0.031 95  PHE   BBB CA  
2799 C  C   . PHE   B 96  ? 0.270 0.024 0.403 0.061  0.033  -0.029 95  PHE   BBB C   
2800 O  O   . PHE   B 96  ? 0.272 0.009 0.404 0.021  0.028  -0.022 95  PHE   BBB O   
2801 C  CB  . PHE   B 96  ? 0.277 0.010 0.351 -0.029 0.035  -0.022 95  PHE   BBB CB  
2802 C  CG  . PHE   B 96  ? 0.318 0.007 0.352 -0.010 -0.009 -0.015 95  PHE   BBB CG  
2803 C  CD1 . PHE   B 96  ? 0.324 0.008 0.359 -0.017 -0.012 -0.020 95  PHE   BBB CD1 
2804 C  CD2 . PHE   B 96  ? 0.295 0.006 0.351 -0.003 -0.023 -0.006 95  PHE   BBB CD2 
2805 C  CE1 . PHE   B 96  ? 0.277 0.010 0.408 0.003  -0.020 0.037  95  PHE   BBB CE1 
2806 C  CE2 . PHE   B 96  ? 0.353 0.011 0.343 0.039  0.003  0.005  95  PHE   BBB CE2 
2807 C  CZ  . PHE   B 96  ? 0.327 0.014 0.416 0.046  -0.015 0.020  95  PHE   BBB CZ  
2808 N  N   . HIS   B 97  ? 0.256 0.029 0.366 -0.061 -0.004 -0.051 96  HIS   BBB N   
2809 C  CA  . HIS   B 97  ? 0.247 0.014 0.369 -0.029 -0.026 -0.037 96  HIS   BBB CA  
2810 C  C   . HIS   B 97  ? 0.297 0.007 0.370 -0.008 0.023  -0.010 96  HIS   BBB C   
2811 O  O   . HIS   B 97  ? 0.307 0.014 0.375 -0.047 0.002  -0.006 96  HIS   BBB O   
2812 C  CB  . HIS   B 97  ? 0.230 0.022 0.376 -0.058 -0.047 0.022  96  HIS   BBB CB  
2813 C  CG  . HIS   B 97  ? 0.231 0.011 0.375 -0.019 -0.031 0.036  96  HIS   BBB CG  
2814 N  ND1 . HIS   B 97  ? 0.317 0.007 0.432 -0.006 0.013  0.008  96  HIS   BBB ND1 
2815 C  CD2 . HIS   B 97  ? 0.290 0.015 0.371 -0.047 0.013  0.017  96  HIS   BBB CD2 
2816 C  CE1 . HIS   B 97  ? 0.279 0.074 0.325 0.038  -0.024 -0.032 96  HIS   BBB CE1 
2817 N  NE2 . HIS   B 97  ? 0.257 0.027 0.342 -0.065 -0.004 0.024  96  HIS   BBB NE2 
2818 N  N   . TRP   B 98  ? 0.268 0.034 0.386 0.044  -0.017 -0.060 97  TRP   BBB N   
2819 C  CA  . TRP   B 98  ? 0.282 0.015 0.420 0.021  -0.004 -0.053 97  TRP   BBB CA  
2820 C  C   . TRP   B 98  ? 0.321 0.015 0.424 -0.047 0.030  -0.032 97  TRP   BBB C   
2821 O  O   . TRP   B 98  ? 0.305 0.028 0.411 -0.056 0.030  -0.044 97  TRP   BBB O   
2822 C  CB  . TRP   B 98  ? 0.244 0.008 0.381 0.002  -0.008 -0.025 97  TRP   BBB CB  
2823 C  CG  . TRP   B 98  ? 0.269 0.008 0.387 0.014  -0.037 -0.023 97  TRP   BBB CG  
2824 C  CD1 . TRP   B 98  ? 0.271 0.070 0.379 -0.003 -0.026 -0.052 97  TRP   BBB CD1 
2825 C  CD2 . TRP   B 98  ? 0.288 0.008 0.397 -0.007 -0.018 -0.020 97  TRP   BBB CD2 
2826 N  NE1 . TRP   B 98  ? 0.330 0.012 0.404 -0.010 -0.030 -0.046 97  TRP   BBB NE1 
2827 C  CE2 . TRP   B 98  ? 0.255 0.011 0.399 -0.025 -0.025 -0.025 97  TRP   BBB CE2 
2828 C  CE3 . TRP   B 98  ? 0.287 0.022 0.375 0.017  -0.028 -0.067 97  TRP   BBB CE3 
2829 C  CZ2 . TRP   B 98  ? 0.267 0.101 0.359 -0.031 -0.025 -0.036 97  TRP   BBB CZ2 
2830 C  CZ3 . TRP   B 98  ? 0.311 0.020 0.392 0.023  -0.020 -0.069 97  TRP   BBB CZ3 
2831 C  CH2 . TRP   B 98  ? 0.267 0.008 0.371 0.015  -0.019 -0.013 97  TRP   BBB CH2 
2832 N  N   . GLY   B 99  ? 0.313 0.012 0.426 -0.043 -0.001 -0.006 98  GLY   BBB N   
2833 C  CA  . GLY   B 99  ? 0.336 0.015 0.491 -0.052 -0.002 0.012  98  GLY   BBB CA  
2834 C  C   . GLY   B 99  ? 0.304 0.009 0.477 -0.013 -0.002 -0.030 98  GLY   BBB C   
2835 O  O   . GLY   B 99  ? 0.324 0.007 0.492 -0.005 -0.012 -0.012 98  GLY   BBB O   
2836 N  N   . SER   B 100 ? 0.448 0.027 0.484 -0.096 0.003  0.004  99  SER   BBB N   
2837 C  CA  A SER   B 100 ? 0.402 0.020 0.538 -0.066 0.006  -0.034 99  SER   BBB CA  
2838 C  CA  B SER   B 100 ? 0.400 0.015 0.547 -0.056 0.002  -0.022 99  SER   BBB CA  
2839 C  C   . SER   B 100 ? 0.411 0.035 0.494 -0.039 -0.024 -0.067 99  SER   BBB C   
2840 O  O   . SER   B 100 ? 0.392 0.192 0.541 -0.069 -0.050 -0.020 99  SER   BBB O   
2841 C  CB  A SER   B 100 ? 0.429 0.037 0.550 -0.103 0.045  -0.063 99  SER   BBB CB  
2842 C  CB  B SER   B 100 ? 0.494 0.026 0.562 -0.098 0.027  -0.014 99  SER   BBB CB  
2843 O  OG  A SER   B 100 ? 0.478 0.199 0.522 -0.041 -0.036 -0.006 99  SER   BBB OG  
2844 O  OG  B SER   B 100 ? 0.472 0.064 0.639 -0.062 0.027  -0.009 99  SER   BBB OG  
2845 N  N   . THR   B 101 ? 0.387 0.033 0.502 -0.058 -0.010 -0.033 100 THR   BBB N   
2846 C  CA  . THR   B 101 ? 0.422 0.199 0.491 -0.149 0.020  -0.069 100 THR   BBB CA  
2847 C  C   . THR   B 101 ? 0.462 0.217 0.416 -0.108 0.049  -0.068 100 THR   BBB C   
2848 O  O   . THR   B 101 ? 0.432 0.183 0.525 -0.114 0.048  -0.103 100 THR   BBB O   
2849 C  CB  . THR   B 101 ? 0.515 0.249 0.497 -0.179 0.102  -0.054 100 THR   BBB CB  
2850 O  OG1 . THR   B 101 ? 0.770 0.132 0.514 -0.083 0.063  0.019  100 THR   BBB OG1 
2851 C  CG2 . THR   B 101 ? 0.535 0.208 0.541 -0.065 0.025  -0.061 100 THR   BBB CG2 
2852 N  N   . ASN   B 102 ? 0.411 0.175 0.496 -0.137 0.053  -0.072 101 ASN   BBB N   
2853 C  CA  . ASN   B 102 ? 0.433 0.207 0.515 -0.086 -0.018 -0.097 101 ASN   BBB CA  
2854 C  C   . ASN   B 102 ? 0.539 0.092 0.523 -0.142 0.001  -0.008 101 ASN   BBB C   
2855 O  O   . ASN   B 102 ? 0.539 0.233 0.498 -0.125 0.028  -0.084 101 ASN   BBB O   
2856 C  CB  . ASN   B 102 ? 0.510 0.145 0.629 -0.024 -0.017 -0.064 101 ASN   BBB CB  
2857 C  CG  . ASN   B 102 ? 0.415 0.286 0.594 -0.021 -0.065 -0.099 101 ASN   BBB CG  
2858 O  OD1 . ASN   B 102 ? 0.518 0.160 0.680 -0.078 0.040  -0.045 101 ASN   BBB OD1 
2859 N  ND2 . ASN   B 102 ? 0.483 0.103 0.761 0.033  0.080  -0.114 101 ASN   BBB ND2 
2860 N  N   . GLU   B 103 ? 0.597 0.078 0.655 -0.151 0.004  -0.086 102 GLU   BBB N   
2861 C  CA  . GLU   B 103 ? 0.521 0.308 0.632 -0.273 -0.087 0.039  102 GLU   BBB CA  
2862 C  C   . GLU   B 103 ? 0.556 0.335 0.454 -0.123 -0.026 -0.054 102 GLU   BBB C   
2863 O  O   . GLU   B 103 ? 0.519 0.406 0.545 -0.105 0.005  0.060  102 GLU   BBB O   
2864 C  CB  . GLU   B 103 ? 0.539 0.212 0.716 -0.207 -0.007 0.154  102 GLU   BBB CB  
2865 C  CG  . GLU   B 103 ? 0.549 0.690 0.881 -0.223 0.004  0.015  102 GLU   BBB CG  
2866 C  CD  . GLU   B 103 ? 0.521 0.788 0.935 -0.148 -0.073 -0.192 102 GLU   BBB CD  
2867 O  OE1 . GLU   B 103 ? 0.839 1.372 0.869 -0.316 0.042  -0.248 102 GLU   BBB OE1 
2868 O  OE2 . GLU   B 103 ? 0.891 0.924 1.322 -0.199 0.387  -0.433 102 GLU   BBB OE2 
2869 N  N   . HIS   B 104 ? 0.427 0.123 0.466 -0.061 -0.041 -0.022 103 HIS   BBB N   
2870 C  CA  . HIS   B 104 ? 0.453 0.066 0.560 0.011  0.000  -0.019 103 HIS   BBB CA  
2871 C  C   . HIS   B 104 ? 0.378 0.192 0.538 -0.162 -0.095 0.040  103 HIS   BBB C   
2872 O  O   . HIS   B 104 ? 0.565 0.167 0.582 -0.063 -0.095 -0.039 103 HIS   BBB O   
2873 C  CB  . HIS   B 104 ? 0.661 0.027 0.689 0.004  -0.047 -0.120 103 HIS   BBB CB  
2874 C  CG  . HIS   B 104 ? 0.668 0.394 0.929 -0.049 -0.084 0.003  103 HIS   BBB CG  
2875 N  ND1 . HIS   B 104 ? 0.956 0.363 1.173 0.118  -0.112 0.063  103 HIS   BBB ND1 
2876 C  CD2 . HIS   B 104 ? 0.581 0.318 0.903 -0.051 -0.079 0.070  103 HIS   BBB CD2 
2877 C  CE1 . HIS   B 104 ? 0.920 0.377 0.860 0.034  0.081  -0.052 103 HIS   BBB CE1 
2878 N  NE2 . HIS   B 104 ? 0.565 0.152 1.040 -0.135 -0.112 0.134  103 HIS   BBB NE2 
2879 N  N   . GLY   B 105 ? 0.406 0.076 0.414 -0.072 -0.043 -0.040 104 GLY   BBB N   
2880 C  CA  . GLY   B 105 ? 0.300 0.119 0.468 0.006  -0.001 0.010  104 GLY   BBB CA  
2881 C  C   . GLY   B 105 ? 0.300 0.018 0.384 0.048  0.010  -0.036 104 GLY   BBB C   
2882 O  O   . GLY   B 105 ? 0.325 0.073 0.425 -0.013 0.005  -0.032 104 GLY   BBB O   
2883 N  N   . SER   B 106 ? 0.266 0.011 0.385 0.029  -0.008 -0.024 105 SER   BBB N   
2884 C  CA  . SER   B 106 ? 0.246 0.077 0.371 0.058  0.007  0.047  105 SER   BBB CA  
2885 C  C   . SER   B 106 ? 0.240 0.007 0.443 -0.006 0.012  -0.017 105 SER   BBB C   
2886 O  O   . SER   B 106 ? 0.290 0.013 0.467 -0.026 0.013  -0.045 105 SER   BBB O   
2887 C  CB  . SER   B 106 ? 0.267 0.014 0.387 0.019  0.031  0.049  105 SER   BBB CB  
2888 O  OG  . SER   B 106 ? 0.390 0.014 0.494 -0.055 0.011  -0.008 105 SER   BBB OG  
2889 N  N   . GLU   B 107 ? 0.248 0.006 0.407 0.003  0.011  0.004  106 GLU   BBB N   
2890 C  CA  . GLU   B 107 ? 0.265 0.008 0.474 -0.023 0.008  -0.004 106 GLU   BBB CA  
2891 C  C   . GLU   B 107 ? 0.311 0.030 0.442 -0.082 -0.006 0.031  106 GLU   BBB C   
2892 O  O   . GLU   B 107 ? 0.324 0.010 0.434 -0.029 0.013  0.020  106 GLU   BBB O   
2893 C  CB  . GLU   B 107 ? 0.284 0.022 0.433 -0.028 0.013  -0.003 106 GLU   BBB CB  
2894 C  CG  . GLU   B 107 ? 0.319 0.007 0.453 -0.002 0.031  0.012  106 GLU   BBB CG  
2895 C  CD  . GLU   B 107 ? 0.228 0.014 0.395 -0.039 -0.050 0.027  106 GLU   BBB CD  
2896 O  OE1 . GLU   B 107 ? 0.343 0.009 0.448 -0.019 -0.032 -0.029 106 GLU   BBB OE1 
2897 O  OE2 . GLU   B 107 ? 0.314 0.008 0.523 -0.020 0.015  -0.018 106 GLU   BBB OE2 
2898 N  N   . HIS   B 108 ? 0.304 0.007 0.392 0.015  -0.034 0.004  107 HIS   BBB N   
2899 C  CA  . HIS   B 108 ? 0.315 0.008 0.379 -0.010 0.019  -0.022 107 HIS   BBB CA  
2900 C  C   . HIS   B 108 ? 0.333 0.010 0.439 -0.035 0.018  0.002  107 HIS   BBB C   
2901 O  O   . HIS   B 108 ? 0.370 0.009 0.503 -0.019 0.028  0.027  107 HIS   BBB O   
2902 C  CB  . HIS   B 108 ? 0.328 0.009 0.418 0.029  -0.003 -0.007 107 HIS   BBB CB  
2903 C  CG  . HIS   B 108 ? 0.301 0.009 0.379 0.025  -0.002 -0.004 107 HIS   BBB CG  
2904 N  ND1 . HIS   B 108 ? 0.346 0.009 0.480 -0.020 0.016  0.025  107 HIS   BBB ND1 
2905 C  CD2 . HIS   B 108 ? 0.295 0.009 0.445 0.016  0.030  0.029  107 HIS   BBB CD2 
2906 C  CE1 . HIS   B 108 ? 0.402 0.020 0.473 -0.043 0.052  0.058  107 HIS   BBB CE1 
2907 N  NE2 . HIS   B 108 ? 0.317 0.015 0.437 -0.052 -0.020 0.013  107 HIS   BBB NE2 
2908 N  N   . THR   B 109 ? 0.405 0.007 0.486 0.009  0.034  0.005  108 THR   BBB N   
2909 C  CA  . THR   B 109 ? 0.413 0.007 0.508 -0.007 0.034  0.016  108 THR   BBB CA  
2910 C  C   . THR   B 109 ? 0.352 0.009 0.487 0.028  0.043  0.005  108 THR   BBB C   
2911 O  O   . THR   B 109 ? 0.336 0.013 0.468 -0.031 0.025  0.041  108 THR   BBB O   
2912 C  CB  . THR   B 109 ? 0.323 0.018 0.514 -0.060 0.049  -0.008 108 THR   BBB CB  
2913 O  OG1 . THR   B 109 ? 0.324 0.053 0.470 -0.015 0.031  0.021  108 THR   BBB OG1 
2914 C  CG2 . THR   B 109 ? 0.384 0.009 0.527 -0.031 0.024  -0.011 108 THR   BBB CG2 
2915 N  N   . VAL   B 110 ? 0.335 0.006 0.457 -0.007 0.027  -0.004 109 VAL   BBB N   
2916 C  CA  . VAL   B 110 ? 0.347 0.018 0.435 -0.002 0.041  0.036  109 VAL   BBB CA  
2917 C  C   . VAL   B 110 ? 0.311 0.091 0.430 -0.025 0.027  0.058  109 VAL   BBB C   
2918 O  O   . VAL   B 110 ? 0.318 0.023 0.489 -0.070 0.035  0.013  109 VAL   BBB O   
2919 C  CB  . VAL   B 110 ? 0.359 0.016 0.405 -0.031 0.014  0.025  109 VAL   BBB CB  
2920 C  CG1 . VAL   B 110 ? 0.388 0.167 0.415 -0.080 0.004  0.008  109 VAL   BBB CG1 
2921 C  CG2 . VAL   B 110 ? 0.337 0.064 0.432 -0.036 -0.010 0.069  109 VAL   BBB CG2 
2922 N  N   . ASP   B 111 ? 0.340 0.066 0.418 -0.065 -0.015 0.075  110 ASP   BBB N   
2923 C  CA  . ASP   B 111 ? 0.352 0.085 0.425 -0.052 0.007  0.103  110 ASP   BBB CA  
2924 C  C   . ASP   B 111 ? 0.340 0.093 0.433 -0.027 0.032  0.058  110 ASP   BBB C   
2925 O  O   . ASP   B 111 ? 0.397 0.047 0.557 -0.073 0.062  0.065  110 ASP   BBB O   
2926 C  CB  . ASP   B 111 ? 0.388 0.017 0.486 -0.031 0.027  0.059  110 ASP   BBB CB  
2927 C  CG  . ASP   B 111 ? 0.356 0.150 0.412 -0.040 0.043  0.054  110 ASP   BBB CG  
2928 O  OD1 . ASP   B 111 ? 0.377 0.235 0.530 -0.038 0.011  0.040  110 ASP   BBB OD1 
2929 O  OD2 . ASP   B 111 ? 0.422 0.164 0.452 -0.037 -0.010 0.019  110 ASP   BBB OD2 
2930 N  N   . GLY   B 112 ? 0.420 0.012 0.465 -0.029 0.084  0.032  111 GLY   BBB N   
2931 C  CA  . GLY   B 112 ? 0.470 0.042 0.553 -0.114 0.035  0.054  111 GLY   BBB CA  
2932 C  C   . GLY   B 112 ? 0.470 0.111 0.560 -0.119 -0.001 -0.022 111 GLY   BBB C   
2933 O  O   . GLY   B 112 ? 0.500 0.065 0.558 -0.078 -0.018 -0.021 111 GLY   BBB O   
2934 N  N   . VAL   B 113 ? 0.391 0.061 0.571 -0.135 -0.021 0.072  112 VAL   BBB N   
2935 C  CA  . VAL   B 113 ? 0.375 0.091 0.498 -0.155 -0.041 0.075  112 VAL   BBB CA  
2936 C  C   . VAL   B 113 ? 0.373 0.047 0.445 -0.060 -0.020 0.058  112 VAL   BBB C   
2937 O  O   . VAL   B 113 ? 0.403 0.016 0.475 -0.042 0.016  0.003  112 VAL   BBB O   
2938 C  CB  . VAL   B 113 ? 0.395 0.137 0.503 -0.023 -0.011 0.086  112 VAL   BBB CB  
2939 C  CG1 . VAL   B 113 ? 0.330 0.211 0.554 -0.035 -0.039 0.058  112 VAL   BBB CG1 
2940 C  CG2 . VAL   B 113 ? 0.406 0.059 0.580 0.001  0.017  0.107  112 VAL   BBB CG2 
2941 N  N   . LYS   B 114 ? 0.395 0.076 0.437 -0.040 -0.022 0.044  113 LYS   BBB N   
2942 C  CA  . LYS   B 114 ? 0.420 0.028 0.449 -0.069 -0.004 0.027  113 LYS   BBB CA  
2943 C  C   . LYS   B 114 ? 0.320 0.077 0.494 -0.068 0.029  0.030  113 LYS   BBB C   
2944 O  O   . LYS   B 114 ? 0.372 0.177 0.511 -0.129 0.061  -0.015 113 LYS   BBB O   
2945 C  CB  . LYS   B 114 ? 0.524 0.088 0.519 -0.003 -0.024 -0.059 113 LYS   BBB CB  
2946 C  CG  . LYS   B 114 ? 0.588 0.101 0.553 0.032  -0.046 0.001  113 LYS   BBB CG  
2947 C  CD  . LYS   B 114 ? 0.755 0.223 0.698 -0.139 0.059  -0.084 113 LYS   BBB CD  
2948 C  CE  . LYS   B 114 ? 1.430 0.020 0.929 -0.001 0.067  -0.019 113 LYS   BBB CE  
2949 N  NZ  . LYS   B 114 ? 1.182 0.433 0.901 -0.318 0.061  -0.299 113 LYS   BBB NZ  
2950 N  N   . TYR   B 115 ? 0.301 0.031 0.456 -0.040 0.020  0.005  114 TYR   BBB N   
2951 C  CA  . TYR   B 115 ? 0.363 0.014 0.454 -0.043 -0.000 -0.033 114 TYR   BBB CA  
2952 C  C   . TYR   B 115 ? 0.238 0.053 0.459 0.032  0.001  -0.010 114 TYR   BBB C   
2953 O  O   . TYR   B 115 ? 0.353 0.007 0.452 0.017  0.029  0.012  114 TYR   BBB O   
2954 C  CB  . TYR   B 115 ? 0.328 0.016 0.437 -0.055 -0.046 -0.009 114 TYR   BBB CB  
2955 C  CG  . TYR   B 115 ? 0.371 0.052 0.443 0.009  0.011  0.018  114 TYR   BBB CG  
2956 C  CD1 . TYR   B 115 ? 0.345 0.014 0.461 -0.027 0.012  0.021  114 TYR   BBB CD1 
2957 C  CD2 . TYR   B 115 ? 0.344 0.100 0.436 0.007  0.013  -0.002 114 TYR   BBB CD2 
2958 C  CE1 . TYR   B 115 ? 0.434 0.158 0.457 -0.010 0.000  0.025  114 TYR   BBB CE1 
2959 C  CE2 . TYR   B 115 ? 0.401 0.099 0.470 -0.006 -0.056 -0.003 114 TYR   BBB CE2 
2960 C  CZ  . TYR   B 115 ? 0.428 0.124 0.456 -0.011 -0.048 0.031  114 TYR   BBB CZ  
2961 O  OH  . TYR   B 115 ? 0.543 0.153 0.467 0.017  0.018  0.058  114 TYR   BBB OH  
2962 N  N   . SER   B 116 ? 0.281 0.011 0.484 -0.020 -0.017 -0.040 115 SER   BBB N   
2963 C  CA  A SER   B 116 ? 0.260 0.014 0.496 -0.015 -0.000 -0.058 115 SER   BBB CA  
2964 C  CA  B SER   B 116 ? 0.264 0.018 0.486 0.010  0.001  -0.072 115 SER   BBB CA  
2965 C  C   . SER   B 116 ? 0.261 0.049 0.451 0.006  -0.007 -0.080 115 SER   BBB C   
2966 O  O   . SER   B 116 ? 0.325 0.045 0.495 -0.045 0.002  -0.094 115 SER   BBB O   
2967 C  CB  A SER   B 116 ? 0.301 0.015 0.503 0.007  0.019  -0.066 115 SER   BBB CB  
2968 C  CB  B SER   B 116 ? 0.367 0.040 0.505 0.060  -0.031 -0.113 115 SER   BBB CB  
2969 O  OG  A SER   B 116 ? 0.320 0.007 0.573 -0.017 0.049  -0.001 115 SER   BBB OG  
2970 O  OG  B SER   B 116 ? 0.455 0.050 0.464 -0.055 -0.025 -0.127 115 SER   BBB OG  
2971 N  N   . ALA   B 117 ? 0.270 0.015 0.438 0.006  0.003  -0.062 116 ALA   BBB N   
2972 C  CA  . ALA   B 117 ? 0.257 0.029 0.403 0.063  0.001  -0.033 116 ALA   BBB CA  
2973 C  C   . ALA   B 117 ? 0.256 0.016 0.384 0.019  0.009  -0.054 116 ALA   BBB C   
2974 O  O   . ALA   B 117 ? 0.312 0.008 0.419 -0.023 0.011  -0.011 116 ALA   BBB O   
2975 C  CB  . ALA   B 117 ? 0.245 0.010 0.417 0.024  -0.023 -0.029 116 ALA   BBB CB  
2976 N  N   . GLU   B 118 ? 0.277 0.016 0.343 0.052  -0.011 -0.000 117 GLU   BBB N   
2977 C  CA  . GLU   B 118 ? 0.263 0.020 0.341 0.047  -0.006 0.037  117 GLU   BBB CA  
2978 C  C   . GLU   B 118 ? 0.300 0.008 0.399 0.019  -0.017 0.007  117 GLU   BBB C   
2979 O  O   . GLU   B 118 ? 0.392 0.007 0.452 -0.016 -0.017 -0.012 117 GLU   BBB O   
2980 C  CB  . GLU   B 118 ? 0.281 0.023 0.442 0.025  -0.029 0.076  117 GLU   BBB CB  
2981 C  CG  . GLU   B 118 ? 0.270 0.017 0.424 0.048  -0.012 0.029  117 GLU   BBB CG  
2982 C  CD  . GLU   B 118 ? 0.259 0.011 0.426 0.011  0.002  0.040  117 GLU   BBB CD  
2983 O  OE1 . GLU   B 118 ? 0.293 0.007 0.521 -0.003 -0.018 0.012  117 GLU   BBB OE1 
2984 O  OE2 . GLU   B 118 ? 0.353 0.007 0.468 -0.009 0.017  -0.003 117 GLU   BBB OE2 
2985 N  N   . LEU   B 119 ? 0.277 0.030 0.334 -0.015 -0.001 -0.032 118 LEU   BBB N   
2986 C  CA  . LEU   B 119 ? 0.321 0.007 0.353 0.014  -0.012 -0.010 118 LEU   BBB CA  
2987 C  C   . LEU   B 119 ? 0.330 0.023 0.430 -0.038 -0.018 -0.071 118 LEU   BBB C   
2988 O  O   . LEU   B 119 ? 0.337 0.010 0.435 -0.028 -0.020 -0.026 118 LEU   BBB O   
2989 C  CB  . LEU   B 119 ? 0.269 0.007 0.407 -0.005 -0.007 -0.015 118 LEU   BBB CB  
2990 C  CG  . LEU   B 119 ? 0.311 0.019 0.374 -0.058 0.003  -0.020 118 LEU   BBB CG  
2991 C  CD1 . LEU   B 119 ? 0.296 0.010 0.399 -0.014 0.006  -0.034 118 LEU   BBB CD1 
2992 C  CD2 . LEU   B 119 ? 0.340 0.008 0.394 -0.021 0.014  -0.005 118 LEU   BBB CD2 
2993 N  N   . HIS   B 120 ? 0.336 0.012 0.435 -0.000 -0.019 -0.049 119 HIS   BBB N   
2994 C  CA  . HIS   B 120 ? 0.338 0.007 0.409 -0.013 -0.022 0.013  119 HIS   BBB CA  
2995 C  C   . HIS   B 120 ? 0.263 0.016 0.341 -0.042 -0.026 0.033  119 HIS   BBB C   
2996 O  O   . HIS   B 120 ? 0.320 0.012 0.363 -0.040 -0.036 0.017  119 HIS   BBB O   
2997 C  CB  . HIS   B 120 ? 0.260 0.011 0.370 -0.002 -0.001 0.041  119 HIS   BBB CB  
2998 C  CG  . HIS   B 120 ? 0.291 0.031 0.361 -0.082 -0.010 0.015  119 HIS   BBB CG  
2999 N  ND1 . HIS   B 120 ? 0.275 0.019 0.636 -0.034 -0.128 0.087  119 HIS   BBB ND1 
3000 C  CD2 . HIS   B 120 ? 0.271 0.010 0.343 -0.031 0.005  0.003  119 HIS   BBB CD2 
3001 C  CE1 . HIS   B 120 ? 0.315 0.053 0.275 0.014  0.006  0.111  119 HIS   BBB CE1 
3002 N  NE2 . HIS   B 120 ? 0.277 0.014 0.348 -0.037 -0.017 0.030  119 HIS   BBB NE2 
3003 N  N   . VAL   B 121 ? 0.303 0.018 0.382 -0.039 -0.046 0.053  120 VAL   BBB N   
3004 C  CA  . VAL   B 121 ? 0.319 0.030 0.332 -0.080 -0.018 0.036  120 VAL   BBB CA  
3005 C  C   . VAL   B 121 ? 0.326 0.043 0.384 -0.107 -0.030 -0.011 120 VAL   BBB C   
3006 O  O   . VAL   B 121 ? 0.369 0.026 0.431 -0.051 -0.073 0.012  120 VAL   BBB O   
3007 C  CB  . VAL   B 121 ? 0.396 0.014 0.352 -0.032 -0.028 0.044  120 VAL   BBB CB  
3008 C  CG1 . VAL   B 121 ? 0.374 0.027 0.472 0.011  -0.009 0.098  120 VAL   BBB CG1 
3009 C  CG2 . VAL   B 121 ? 0.408 0.015 0.463 -0.051 -0.047 -0.026 120 VAL   BBB CG2 
3010 N  N   . ALA   B 122 ? 0.310 0.016 0.406 -0.051 -0.033 0.020  121 ALA   BBB N   
3011 C  CA  . ALA   B 122 ? 0.290 0.016 0.407 -0.049 -0.026 0.031  121 ALA   BBB CA  
3012 C  C   . ALA   B 122 ? 0.269 0.033 0.436 -0.044 -0.051 0.098  121 ALA   BBB C   
3013 O  O   . ALA   B 122 ? 0.373 0.023 0.490 -0.067 -0.036 0.051  121 ALA   BBB O   
3014 C  CB  . ALA   B 122 ? 0.289 0.009 0.432 0.023  -0.026 0.015  121 ALA   BBB CB  
3015 N  N   . HIS   B 123 ? 0.288 0.026 0.417 -0.044 -0.067 0.082  122 HIS   BBB N   
3016 C  CA  . HIS   B 123 ? 0.313 0.050 0.400 -0.083 -0.055 0.088  122 HIS   BBB CA  
3017 C  C   . HIS   B 123 ? 0.343 0.028 0.474 -0.057 -0.058 0.080  122 HIS   BBB C   
3018 O  O   . HIS   B 123 ? 0.346 0.038 0.478 -0.047 -0.043 0.107  122 HIS   BBB O   
3019 C  CB  . HIS   B 123 ? 0.303 0.030 0.393 -0.048 0.009  0.078  122 HIS   BBB CB  
3020 C  CG  . HIS   B 123 ? 0.286 0.014 0.426 -0.044 0.004  0.019  122 HIS   BBB CG  
3021 N  ND1 . HIS   B 123 ? 0.364 0.039 0.437 -0.079 -0.034 0.090  122 HIS   BBB ND1 
3022 C  CD2 . HIS   B 123 ? 0.376 0.033 0.473 -0.034 -0.057 0.110  122 HIS   BBB CD2 
3023 C  CE1 . HIS   B 123 ? 0.352 0.061 0.404 -0.133 -0.045 0.055  122 HIS   BBB CE1 
3024 N  NE2 . HIS   B 123 ? 0.382 0.027 0.359 -0.085 -0.045 0.029  122 HIS   BBB NE2 
3025 N  N   . TRP   B 124 ? 0.356 0.125 0.457 -0.109 -0.063 0.066  123 TRP   BBB N   
3026 C  CA  . TRP   B 124 ? 0.373 0.073 0.489 -0.099 -0.078 0.147  123 TRP   BBB CA  
3027 C  C   . TRP   B 124 ? 0.276 0.150 0.442 -0.045 -0.021 0.077  123 TRP   BBB C   
3028 O  O   . TRP   B 124 ? 0.440 0.083 0.507 -0.134 -0.071 0.062  123 TRP   BBB O   
3029 C  CB  . TRP   B 124 ? 0.350 0.096 0.487 -0.093 -0.085 0.142  123 TRP   BBB CB  
3030 C  CG  . TRP   B 124 ? 0.390 0.135 0.544 -0.136 -0.109 0.187  123 TRP   BBB CG  
3031 C  CD1 . TRP   B 124 ? 0.373 0.087 0.531 -0.092 -0.057 0.155  123 TRP   BBB CD1 
3032 C  CD2 . TRP   B 124 ? 0.358 0.306 0.634 -0.156 -0.101 0.203  123 TRP   BBB CD2 
3033 N  NE1 . TRP   B 124 ? 0.468 0.133 0.603 -0.138 -0.096 0.211  123 TRP   BBB NE1 
3034 C  CE2 . TRP   B 124 ? 0.456 0.214 0.714 -0.149 -0.071 0.214  123 TRP   BBB CE2 
3035 C  CE3 . TRP   B 124 ? 0.379 0.246 0.712 -0.107 -0.045 0.192  123 TRP   BBB CE3 
3036 C  CZ2 . TRP   B 124 ? 0.480 0.470 0.617 -0.217 -0.045 0.334  123 TRP   BBB CZ2 
3037 C  CZ3 . TRP   B 124 ? 0.463 0.537 0.695 -0.280 -0.069 0.267  123 TRP   BBB CZ3 
3038 C  CH2 . TRP   B 124 ? 0.510 0.483 0.830 -0.427 -0.063 0.360  123 TRP   BBB CH2 
3039 N  N   . ASN   B 125 ? 0.298 0.195 0.548 -0.053 -0.069 0.165  124 ASN   BBB N   
3040 C  CA  . ASN   B 125 ? 0.288 0.223 0.552 -0.109 -0.057 0.166  124 ASN   BBB CA  
3041 C  C   . ASN   B 125 ? 0.275 0.367 0.484 -0.138 0.001  0.147  124 ASN   BBB C   
3042 O  O   . ASN   B 125 ? 0.332 0.238 0.596 -0.100 -0.003 0.119  124 ASN   BBB O   
3043 C  CB  . ASN   B 125 ? 0.361 0.203 0.557 -0.133 -0.076 0.192  124 ASN   BBB CB  
3044 C  CG  . ASN   B 125 ? 0.323 0.374 0.518 -0.054 -0.079 0.146  124 ASN   BBB CG  
3045 O  OD1 . ASN   B 125 ? 0.428 0.452 0.632 -0.089 -0.145 0.207  124 ASN   BBB OD1 
3046 N  ND2 . ASN   B 125 ? 0.396 0.426 0.528 -0.155 -0.116 0.206  124 ASN   BBB ND2 
3047 N  N   . SER   B 126 ? 0.442 0.338 0.582 -0.159 -0.093 0.213  125 SER   BBB N   
3048 C  CA  . SER   B 126 ? 0.504 0.404 0.690 -0.204 -0.068 0.264  125 SER   BBB CA  
3049 C  C   . SER   B 126 ? 0.488 0.549 0.746 -0.178 -0.113 0.268  125 SER   BBB C   
3050 O  O   . SER   B 126 ? 0.688 0.527 0.722 -0.326 -0.089 0.214  125 SER   BBB O   
3051 C  CB  . SER   B 126 ? 0.622 0.456 0.820 -0.025 -0.003 0.164  125 SER   BBB CB  
3052 O  OG  . SER   B 126 ? 0.614 0.271 0.721 -0.206 -0.062 0.172  125 SER   BBB OG  
3053 N  N   . ALA   B 127 ? 0.613 0.336 0.767 -0.187 -0.154 0.198  126 ALA   BBB N   
3054 C  CA  . ALA   B 127 ? 0.510 0.337 0.769 -0.108 -0.131 0.239  126 ALA   BBB CA  
3055 C  C   . ALA   B 127 ? 0.483 0.416 0.650 -0.225 -0.119 0.145  126 ALA   BBB C   
3056 O  O   . ALA   B 127 ? 0.479 0.430 0.790 -0.276 -0.180 0.172  126 ALA   BBB O   
3057 C  CB  . ALA   B 127 ? 0.590 0.207 0.753 -0.084 -0.191 0.171  126 ALA   BBB CB  
3058 N  N   . LYS   B 128 ? 0.386 0.375 0.563 -0.155 -0.066 0.131  127 LYS   BBB N   
3059 C  CA  . LYS   B 128 ? 0.421 0.493 0.644 -0.114 -0.090 0.169  127 LYS   BBB CA  
3060 C  C   . LYS   B 128 ? 0.398 0.605 0.626 -0.071 -0.073 0.166  127 LYS   BBB C   
3061 O  O   . LYS   B 128 ? 0.405 0.540 0.653 -0.120 -0.020 0.213  127 LYS   BBB O   
3062 C  CB  . LYS   B 128 ? 0.426 0.526 0.688 -0.067 -0.096 0.283  127 LYS   BBB CB  
3063 C  CG  . LYS   B 128 ? 0.498 0.751 0.695 -0.092 -0.183 0.216  127 LYS   BBB CG  
3064 C  CD  . LYS   B 128 ? 0.610 0.793 1.053 0.018  -0.105 0.289  127 LYS   BBB CD  
3065 C  CE  . LYS   B 128 ? 0.555 0.955 1.019 -0.296 -0.230 0.238  127 LYS   BBB CE  
3066 N  NZ  . LYS   B 128 ? 0.481 1.276 1.109 -0.226 -0.236 0.404  127 LYS   BBB NZ  
3067 N  N   . TYR   B 129 ? 0.432 0.434 0.550 -0.155 -0.106 0.196  128 TYR   BBB N   
3068 C  CA  . TYR   B 129 ? 0.378 0.260 0.557 -0.055 -0.088 0.164  128 TYR   BBB CA  
3069 C  C   . TYR   B 129 ? 0.416 0.234 0.651 -0.119 -0.118 0.210  128 TYR   BBB C   
3070 O  O   . TYR   B 129 ? 0.415 0.373 0.654 -0.199 -0.029 0.128  128 TYR   BBB O   
3071 C  CB  . TYR   B 129 ? 0.339 0.287 0.657 -0.067 -0.063 0.175  128 TYR   BBB CB  
3072 C  CG  . TYR   B 129 ? 0.385 0.420 0.674 -0.066 -0.011 0.292  128 TYR   BBB CG  
3073 C  CD1 . TYR   B 129 ? 0.347 0.464 0.742 -0.114 -0.034 0.320  128 TYR   BBB CD1 
3074 C  CD2 . TYR   B 129 ? 0.358 0.331 0.664 -0.106 -0.023 0.248  128 TYR   BBB CD2 
3075 C  CE1 . TYR   B 129 ? 0.429 0.662 0.706 -0.074 -0.061 0.394  128 TYR   BBB CE1 
3076 C  CE2 . TYR   B 129 ? 0.366 0.556 0.717 -0.073 -0.015 0.366  128 TYR   BBB CE2 
3077 C  CZ  . TYR   B 129 ? 0.344 0.560 0.744 -0.093 -0.088 0.351  128 TYR   BBB CZ  
3078 O  OH  . TYR   B 129 ? 0.416 0.461 0.803 -0.061 -0.111 0.292  128 TYR   BBB OH  
3079 N  N   . SER   B 130 ? 0.502 0.454 0.681 -0.235 -0.082 0.182  129 SER   BBB N   
3080 C  CA  . SER   B 130 ? 0.404 0.523 0.690 -0.115 -0.040 0.174  129 SER   BBB CA  
3081 C  C   . SER   B 130 ? 0.455 0.655 0.744 -0.279 -0.065 0.124  129 SER   BBB C   
3082 O  O   . SER   B 130 ? 0.734 0.579 0.911 -0.155 -0.200 0.255  129 SER   BBB O   
3083 C  CB  . SER   B 130 ? 0.427 0.292 0.588 -0.157 -0.044 0.074  129 SER   BBB CB  
3084 O  OG  . SER   B 130 ? 0.451 0.221 0.581 -0.041 -0.055 0.051  129 SER   BBB OG  
3085 N  N   . SER   B 131 ? 0.410 0.521 0.686 -0.117 -0.077 0.228  130 SER   BBB N   
3086 C  CA  . SER   B 131 ? 0.547 0.489 0.685 -0.261 -0.126 0.254  130 SER   BBB CA  
3087 C  C   . SER   B 131 ? 0.611 0.557 0.776 -0.393 -0.090 0.233  130 SER   BBB C   
3088 O  O   . SER   B 131 ? 0.461 0.439 0.695 -0.212 -0.073 0.301  130 SER   BBB O   
3089 C  CB  . SER   B 131 ? 0.463 0.375 0.774 -0.346 -0.126 0.292  130 SER   BBB CB  
3090 O  OG  . SER   B 131 ? 0.544 0.534 0.635 -0.144 -0.130 0.305  130 SER   BBB OG  
3091 N  N   . LEU   B 132 ? 0.623 0.538 0.844 -0.337 -0.105 0.185  131 LEU   BBB N   
3092 C  CA  . LEU   B 132 ? 0.470 0.412 0.539 -0.168 -0.135 0.159  131 LEU   BBB CA  
3093 C  C   . LEU   B 132 ? 0.396 0.544 0.537 -0.131 -0.049 0.164  131 LEU   BBB C   
3094 O  O   . LEU   B 132 ? 0.432 0.345 0.512 -0.094 0.008  0.073  131 LEU   BBB O   
3095 C  CB  . LEU   B 132 ? 0.446 0.360 0.574 -0.201 -0.107 0.232  131 LEU   BBB CB  
3096 C  CG  . LEU   B 132 ? 0.500 0.286 0.536 -0.269 -0.132 0.091  131 LEU   BBB CG  
3097 C  CD1 . LEU   B 132 ? 0.398 0.094 0.541 -0.092 -0.074 0.098  131 LEU   BBB CD1 
3098 C  CD2 . LEU   B 132 ? 0.459 0.399 0.570 -0.167 -0.043 0.159  131 LEU   BBB CD2 
3099 N  N   . ALA   B 133 ? 0.521 0.180 0.556 -0.192 -0.022 0.045  132 ALA   BBB N   
3100 C  CA  . ALA   B 133 ? 0.428 0.544 0.496 -0.069 0.037  -0.038 132 ALA   BBB CA  
3101 C  C   . ALA   B 133 ? 0.389 0.509 0.548 -0.108 0.029  0.052  132 ALA   BBB C   
3102 O  O   . ALA   B 133 ? 0.503 0.568 0.579 -0.139 0.041  -0.007 132 ALA   BBB O   
3103 C  CB  . ALA   B 133 ? 0.607 0.805 0.544 -0.093 0.079  0.016  132 ALA   BBB CB  
3104 N  N   . GLU   B 134 ? 0.421 0.690 0.475 -0.192 -0.036 0.102  133 GLU   BBB N   
3105 C  CA  . GLU   B 134 ? 0.431 0.603 0.518 -0.179 -0.049 0.111  133 GLU   BBB CA  
3106 C  C   . GLU   B 134 ? 0.401 0.503 0.536 -0.167 -0.051 0.124  133 GLU   BBB C   
3107 O  O   . GLU   B 134 ? 0.498 0.438 0.570 -0.151 -0.016 0.054  133 GLU   BBB O   
3108 C  CB  . GLU   B 134 ? 0.467 0.424 0.586 -0.121 -0.052 0.221  133 GLU   BBB CB  
3109 C  CG  . GLU   B 134 ? 0.477 0.142 0.614 -0.015 -0.037 0.083  133 GLU   BBB CG  
3110 C  CD  . GLU   B 134 ? 0.502 0.414 0.595 -0.174 -0.147 0.152  133 GLU   BBB CD  
3111 O  OE1 . GLU   B 134 ? 0.452 0.575 0.715 -0.198 -0.174 0.249  133 GLU   BBB OE1 
3112 O  OE2 . GLU   B 134 ? 0.450 0.424 0.870 -0.074 -0.056 0.116  133 GLU   BBB OE2 
3113 N  N   . ALA   B 135 ? 0.373 0.546 0.528 -0.176 0.001  0.178  134 ALA   BBB N   
3114 C  CA  . ALA   B 135 ? 0.407 0.498 0.495 -0.106 -0.028 0.151  134 ALA   BBB CA  
3115 C  C   . ALA   B 135 ? 0.345 0.520 0.483 -0.092 0.017  0.142  134 ALA   BBB C   
3116 O  O   . ALA   B 135 ? 0.422 0.401 0.596 -0.151 0.001  0.182  134 ALA   BBB O   
3117 C  CB  . ALA   B 135 ? 0.431 0.504 0.499 -0.144 -0.056 0.096  134 ALA   BBB CB  
3118 N  N   . ALA   B 136 ? 0.403 0.511 0.453 -0.124 0.012  0.149  135 ALA   BBB N   
3119 C  CA  . ALA   B 136 ? 0.392 0.483 0.426 -0.100 0.071  0.079  135 ALA   BBB CA  
3120 C  C   . ALA   B 136 ? 0.305 0.521 0.513 -0.051 -0.018 0.108  135 ALA   BBB C   
3121 O  O   . ALA   B 136 ? 0.425 0.438 0.492 -0.016 0.074  0.107  135 ALA   BBB O   
3122 C  CB  . ALA   B 136 ? 0.518 0.478 0.428 -0.093 0.039  0.100  135 ALA   BBB CB  
3123 N  N   . SER   B 137 ? 0.339 0.282 0.534 -0.054 0.024  0.082  136 SER   BBB N   
3124 C  CA  . SER   B 137 ? 0.445 0.337 0.559 0.014  0.029  0.051  136 SER   BBB CA  
3125 C  C   . SER   B 137 ? 0.414 0.381 0.562 0.011  0.025  0.102  136 SER   BBB C   
3126 O  O   . SER   B 137 ? 0.645 0.425 0.650 0.026  0.008  0.242  136 SER   BBB O   
3127 C  CB  . SER   B 137 ? 0.435 0.153 0.678 0.026  0.047  0.034  136 SER   BBB CB  
3128 O  OG  . SER   B 137 ? 0.486 0.586 0.590 -0.108 0.068  0.080  136 SER   BBB OG  
3129 N  N   . LYS   B 138 ? 0.410 0.399 0.501 -0.060 -0.020 0.100  137 LYS   BBB N   
3130 C  CA  . LYS   B 138 ? 0.409 0.496 0.466 -0.053 0.020  0.096  137 LYS   BBB CA  
3131 C  C   . LYS   B 138 ? 0.281 0.382 0.465 -0.022 0.006  0.074  137 LYS   BBB C   
3132 O  O   . LYS   B 138 ? 0.305 0.281 0.495 0.017  0.043  0.013  137 LYS   BBB O   
3133 C  CB  . LYS   B 138 ? 0.437 0.407 0.554 -0.018 -0.013 0.165  137 LYS   BBB CB  
3134 C  CG  . LYS   B 138 ? 0.537 0.537 0.519 0.040  0.019  0.165  137 LYS   BBB CG  
3135 C  CD  . LYS   B 138 ? 0.540 0.645 0.538 0.058  0.036  0.193  137 LYS   BBB CD  
3136 C  CE  . LYS   B 138 ? 0.685 0.629 0.480 0.109  0.064  0.241  137 LYS   BBB CE  
3137 N  NZ  . LYS   B 138 ? 0.819 0.459 0.502 0.147  0.144  0.133  137 LYS   BBB NZ  
3138 N  N   . ALA   B 139 ? 0.381 0.433 0.474 -0.009 -0.039 0.057  138 ALA   BBB N   
3139 C  CA  . ALA   B 139 ? 0.362 0.391 0.469 0.039  0.016  0.025  138 ALA   BBB CA  
3140 C  C   . ALA   B 139 ? 0.287 0.255 0.435 0.032  -0.011 0.105  138 ALA   BBB C   
3141 O  O   . ALA   B 139 ? 0.334 0.361 0.494 -0.014 0.030  0.055  138 ALA   BBB O   
3142 C  CB  . ALA   B 139 ? 0.450 0.304 0.434 0.032  -0.016 0.001  138 ALA   BBB CB  
3143 N  N   . ASP   B 140 ? 0.359 0.335 0.471 -0.029 -0.012 0.074  139 ASP   BBB N   
3144 C  CA  . ASP   B 140 ? 0.326 0.242 0.472 0.001  -0.007 0.123  139 ASP   BBB CA  
3145 C  C   . ASP   B 140 ? 0.319 0.324 0.453 -0.031 -0.054 0.149  139 ASP   BBB C   
3146 O  O   . ASP   B 140 ? 0.450 0.284 0.517 -0.126 -0.014 0.154  139 ASP   BBB O   
3147 C  CB  . ASP   B 140 ? 0.350 0.207 0.540 -0.009 -0.027 0.115  139 ASP   BBB CB  
3148 C  CG  . ASP   B 140 ? 0.401 0.309 0.507 -0.073 -0.051 0.192  139 ASP   BBB CG  
3149 O  OD1 . ASP   B 140 ? 0.438 0.403 0.561 -0.171 -0.085 0.238  139 ASP   BBB OD1 
3150 O  OD2 . ASP   B 140 ? 0.451 0.370 0.628 -0.144 0.000  0.080  139 ASP   BBB OD2 
3151 N  N   . GLY   B 141 ? 0.310 0.393 0.442 -0.020 -0.044 0.184  140 GLY   BBB N   
3152 C  CA  . GLY   B 141 ? 0.289 0.236 0.455 -0.080 -0.008 0.148  140 GLY   BBB CA  
3153 C  C   . GLY   B 141 ? 0.304 0.262 0.432 -0.091 0.025  0.078  140 GLY   BBB C   
3154 O  O   . GLY   B 141 ? 0.363 0.262 0.563 -0.155 -0.063 0.102  140 GLY   BBB O   
3155 N  N   . LEU   B 142 ? 0.315 0.160 0.483 -0.065 -0.010 0.107  141 LEU   BBB N   
3156 C  CA  . LEU   B 142 ? 0.333 0.070 0.428 -0.077 -0.027 0.094  141 LEU   BBB CA  
3157 C  C   . LEU   B 142 ? 0.314 0.164 0.468 -0.017 0.005  0.109  141 LEU   BBB C   
3158 O  O   . LEU   B 142 ? 0.348 0.076 0.430 -0.038 -0.009 0.059  141 LEU   BBB O   
3159 C  CB  . LEU   B 142 ? 0.412 0.016 0.435 -0.027 -0.036 0.059  141 LEU   BBB CB  
3160 C  CG  . LEU   B 142 ? 0.420 0.031 0.461 -0.045 -0.010 0.095  141 LEU   BBB CG  
3161 C  CD1 . LEU   B 142 ? 0.370 0.197 0.437 -0.036 -0.021 0.055  141 LEU   BBB CD1 
3162 C  CD2 . LEU   B 142 ? 0.422 0.030 0.507 -0.040 -0.020 0.102  141 LEU   BBB CD2 
3163 N  N   . ALA   B 143 ? 0.364 0.025 0.423 -0.041 -0.023 0.078  142 ALA   BBB N   
3164 C  CA  . ALA   B 143 ? 0.321 0.092 0.393 -0.076 -0.036 0.083  142 ALA   BBB CA  
3165 C  C   . ALA   B 143 ? 0.318 0.133 0.362 -0.091 -0.048 0.132  142 ALA   BBB C   
3166 O  O   . ALA   B 143 ? 0.323 0.021 0.402 -0.048 -0.039 0.061  142 ALA   BBB O   
3167 C  CB  . ALA   B 143 ? 0.363 0.076 0.480 -0.085 -0.047 0.046  142 ALA   BBB CB  
3168 N  N   . VAL   B 144 ? 0.311 0.015 0.433 -0.022 -0.029 0.058  143 VAL   BBB N   
3169 C  CA  . VAL   B 144 ? 0.293 0.008 0.362 -0.016 -0.046 0.018  143 VAL   BBB CA  
3170 C  C   . VAL   B 144 ? 0.284 0.024 0.379 0.050  -0.045 -0.007 143 VAL   BBB C   
3171 O  O   . VAL   B 144 ? 0.323 0.008 0.404 -0.025 -0.034 0.000  143 VAL   BBB O   
3172 C  CB  . VAL   B 144 ? 0.353 0.021 0.356 -0.070 -0.046 0.025  143 VAL   BBB CB  
3173 C  CG1 . VAL   B 144 ? 0.355 0.030 0.538 -0.076 -0.058 -0.049 143 VAL   BBB CG1 
3174 C  CG2 . VAL   B 144 ? 0.372 0.033 0.407 0.005  -0.012 0.103  143 VAL   BBB CG2 
3175 N  N   . ILE   B 145 ? 0.334 0.008 0.450 -0.023 -0.028 0.015  144 ILE   BBB N   
3176 C  CA  . ILE   B 145 ? 0.321 0.008 0.436 0.024  -0.039 0.002  144 ILE   BBB CA  
3177 C  C   . ILE   B 145 ? 0.311 0.028 0.355 -0.052 0.002  0.065  144 ILE   BBB C   
3178 O  O   . ILE   B 145 ? 0.381 0.024 0.426 -0.060 -0.022 0.061  144 ILE   BBB O   
3179 C  CB  . ILE   B 145 ? 0.348 0.012 0.455 0.042  -0.039 -0.012 144 ILE   BBB CB  
3180 C  CG1 . ILE   B 145 ? 0.317 0.017 0.492 0.030  -0.046 0.057  144 ILE   BBB CG1 
3181 C  CG2 . ILE   B 145 ? 0.353 0.015 0.458 0.045  -0.042 0.032  144 ILE   BBB CG2 
3182 C  CD1 . ILE   B 145 ? 0.361 0.026 0.496 0.064  -0.022 0.058  144 ILE   BBB CD1 
3183 N  N   . GLY   B 146 ? 0.335 0.011 0.441 -0.010 -0.014 0.046  145 GLY   BBB N   
3184 C  CA  . GLY   B 146 ? 0.310 0.011 0.428 -0.006 -0.040 0.043  145 GLY   BBB CA  
3185 C  C   . GLY   B 146 ? 0.324 0.014 0.497 -0.050 -0.045 0.013  145 GLY   BBB C   
3186 O  O   . GLY   B 146 ? 0.322 0.009 0.498 -0.028 -0.011 -0.006 145 GLY   BBB O   
3187 N  N   . VAL   B 147 ? 0.308 0.023 0.371 -0.067 -0.026 0.033  146 VAL   BBB N   
3188 C  CA  . VAL   B 147 ? 0.286 0.012 0.393 0.011  -0.038 0.044  146 VAL   BBB CA  
3189 C  C   . VAL   B 147 ? 0.256 0.016 0.304 0.013  -0.005 -0.014 146 VAL   BBB C   
3190 O  O   . VAL   B 147 ? 0.286 0.008 0.341 0.000  -0.031 0.021  146 VAL   BBB O   
3191 C  CB  . VAL   B 147 ? 0.297 0.024 0.378 0.010  -0.011 0.081  146 VAL   BBB CB  
3192 C  CG1 . VAL   B 147 ? 0.297 0.017 0.458 -0.039 0.010  0.048  146 VAL   BBB CG1 
3193 C  CG2 . VAL   B 147 ? 0.279 0.009 0.381 0.022  -0.011 0.012  146 VAL   BBB CG2 
3194 N  N   . LEU   B 148 ? 0.254 0.006 0.338 0.006  0.002  -0.002 147 LEU   BBB N   
3195 C  CA  . LEU   B 148 ? 0.246 0.022 0.339 -0.001 -0.009 -0.024 147 LEU   BBB CA  
3196 C  C   . LEU   B 148 ? 0.260 0.022 0.334 0.007  -0.033 -0.017 147 LEU   BBB C   
3197 O  O   . LEU   B 148 ? 0.330 0.026 0.353 -0.026 -0.022 -0.038 147 LEU   BBB O   
3198 C  CB  . LEU   B 148 ? 0.297 0.068 0.360 0.002  -0.005 0.014  147 LEU   BBB CB  
3199 C  CG  . LEU   B 148 ? 0.289 0.067 0.444 -0.015 -0.011 0.018  147 LEU   BBB CG  
3200 C  CD1 . LEU   B 148 ? 0.392 0.100 0.472 0.019  -0.012 0.038  147 LEU   BBB CD1 
3201 C  CD2 . LEU   B 148 ? 0.404 0.047 0.461 0.056  0.033  0.014  147 LEU   BBB CD2 
3202 N  N   . MET   B 149 ? 0.315 0.011 0.390 -0.020 -0.023 -0.032 148 MET   BBB N   
3203 C  CA  . MET   B 149 ? 0.333 0.010 0.431 -0.012 -0.007 -0.039 148 MET   BBB CA  
3204 C  C   . MET   B 149 ? 0.290 0.010 0.378 0.022  0.036  -0.024 148 MET   BBB C   
3205 O  O   . MET   B 149 ? 0.299 0.018 0.472 -0.018 0.020  -0.070 148 MET   BBB O   
3206 C  CB  . MET   B 149 ? 0.325 0.008 0.445 0.022  0.030  -0.012 148 MET   BBB CB  
3207 C  CG  . MET   B 149 ? 0.269 0.011 0.469 0.026  0.020  -0.032 148 MET   BBB CG  
3208 S  SD  . MET   B 149 ? 0.311 0.007 0.430 0.014  -0.016 -0.010 148 MET   BBB SD  
3209 C  CE  . MET   B 149 ? 0.291 0.098 0.457 0.032  -0.023 -0.015 148 MET   BBB CE  
3210 N  N   . LYS   B 150 ? 0.269 0.011 0.370 0.028  0.010  -0.021 149 LYS   BBB N   
3211 C  CA  . LYS   B 150 ? 0.271 0.018 0.411 0.042  0.043  -0.005 149 LYS   BBB CA  
3212 C  C   . LYS   B 150 ? 0.277 0.048 0.408 0.028  0.015  -0.008 149 LYS   BBB C   
3213 O  O   . LYS   B 150 ? 0.314 0.054 0.396 0.055  0.013  0.012  149 LYS   BBB O   
3214 C  CB  . LYS   B 150 ? 0.351 0.078 0.429 0.053  0.019  0.027  149 LYS   BBB CB  
3215 C  CG  . LYS   B 150 ? 0.397 0.122 0.469 0.060  0.061  0.079  149 LYS   BBB CG  
3216 C  CD  . LYS   B 150 ? 0.536 0.282 0.483 0.049  0.057  0.058  149 LYS   BBB CD  
3217 C  CE  . LYS   B 150 ? 0.666 0.499 0.510 0.015  0.172  0.159  149 LYS   BBB CE  
3218 N  NZ  . LYS   B 150 ? 0.908 0.723 0.666 0.028  0.120  -0.057 149 LYS   BBB NZ  
3219 N  N   . VAL   B 151 ? 0.306 0.060 0.385 0.002  0.015  -0.000 150 VAL   BBB N   
3220 C  CA  . VAL   B 151 ? 0.330 0.072 0.376 -0.004 0.013  0.049  150 VAL   BBB CA  
3221 C  C   . VAL   B 151 ? 0.325 0.032 0.428 0.026  0.037  0.079  150 VAL   BBB C   
3222 O  O   . VAL   B 151 ? 0.356 0.103 0.397 0.058  0.061  0.034  150 VAL   BBB O   
3223 C  CB  . VAL   B 151 ? 0.362 0.132 0.446 0.009  0.000  -0.014 150 VAL   BBB CB  
3224 C  CG1 . VAL   B 151 ? 0.337 0.153 0.429 0.043  -0.001 0.016  150 VAL   BBB CG1 
3225 C  CG2 . VAL   B 151 ? 0.410 0.079 0.531 -0.036 -0.011 0.079  150 VAL   BBB CG2 
3226 N  N   . GLY   B 152 ? 0.324 0.018 0.389 0.018  0.021  0.055  151 GLY   BBB N   
3227 C  CA  . GLY   B 152 ? 0.311 0.190 0.408 0.037  0.027  0.054  151 GLY   BBB CA  
3228 C  C   . GLY   B 152 ? 0.364 0.125 0.399 0.051  -0.010 -0.015 151 GLY   BBB C   
3229 O  O   . GLY   B 152 ? 0.356 0.128 0.428 0.023  -0.008 -0.023 151 GLY   BBB O   
3230 N  N   . GLU   B 153 ? 0.477 0.030 0.430 0.076  0.041  0.039  152 GLU   BBB N   
3231 C  CA  . GLU   B 153 ? 0.439 0.058 0.479 0.096  0.028  0.075  152 GLU   BBB CA  
3232 C  C   . GLU   B 153 ? 0.360 0.020 0.416 0.068  -0.021 -0.024 152 GLU   BBB C   
3233 O  O   . GLU   B 153 ? 0.345 0.083 0.475 0.070  -0.014 0.018  152 GLU   BBB O   
3234 C  CB  . GLU   B 153 ? 0.609 0.164 0.475 0.087  0.028  0.030  152 GLU   BBB CB  
3235 C  CG  . GLU   B 153 ? 0.721 0.390 0.644 -0.013 0.105  0.191  152 GLU   BBB CG  
3236 C  CD  . GLU   B 153 ? 0.736 0.646 0.872 -0.010 0.112  0.198  152 GLU   BBB CD  
3237 O  OE1 . GLU   B 153 ? 0.705 0.829 0.998 0.208  0.364  0.279  152 GLU   BBB OE1 
3238 O  OE2 . GLU   B 153 ? 1.077 1.089 0.987 -0.119 0.137  0.618  152 GLU   BBB OE2 
3239 N  N   . ALA   B 154 ? 0.360 0.149 0.367 0.089  -0.016 0.007  153 ALA   BBB N   
3240 C  CA  . ALA   B 154 ? 0.329 0.173 0.345 0.080  -0.012 -0.031 153 ALA   BBB CA  
3241 C  C   . ALA   B 154 ? 0.332 0.191 0.369 0.067  -0.002 -0.025 153 ALA   BBB C   
3242 O  O   . ALA   B 154 ? 0.409 0.144 0.403 0.089  0.035  -0.033 153 ALA   BBB O   
3243 C  CB  . ALA   B 154 ? 0.326 0.106 0.450 0.083  -0.012 -0.002 153 ALA   BBB CB  
3244 N  N   . ASN   B 155 ? 0.349 0.028 0.408 0.083  0.004  -0.024 154 ASN   BBB N   
3245 C  CA  . ASN   B 155 ? 0.300 0.142 0.406 0.075  -0.026 0.010  154 ASN   BBB CA  
3246 C  C   . ASN   B 155 ? 0.383 0.040 0.393 0.099  -0.014 -0.058 154 ASN   BBB C   
3247 O  O   . ASN   B 155 ? 0.372 0.021 0.414 0.072  -0.004 -0.015 154 ASN   BBB O   
3248 C  CB  . ASN   B 155 ? 0.321 0.014 0.519 0.044  -0.030 -0.031 154 ASN   BBB CB  
3249 C  CG  . ASN   B 155 ? 0.318 0.011 0.437 0.035  -0.019 -0.021 154 ASN   BBB CG  
3250 O  OD1 . ASN   B 155 ? 0.490 0.047 0.531 0.122  -0.107 -0.097 154 ASN   BBB OD1 
3251 N  ND2 . ASN   B 155 ? 0.353 0.016 0.426 0.059  -0.051 -0.009 154 ASN   BBB ND2 
3252 N  N   . PRO   B 156 ? 0.465 0.021 0.429 0.074  0.007  -0.032 155 PRO   BBB N   
3253 C  CA  . PRO   B 156 ? 0.433 0.085 0.428 0.180  -0.009 0.028  155 PRO   BBB CA  
3254 C  C   . PRO   B 156 ? 0.432 0.180 0.331 0.084  -0.026 -0.069 155 PRO   BBB C   
3255 O  O   . PRO   B 156 ? 0.448 0.103 0.407 0.100  -0.037 -0.009 155 PRO   BBB O   
3256 C  CB  . PRO   B 156 ? 0.504 0.151 0.571 0.219  0.028  -0.039 155 PRO   BBB CB  
3257 C  CG  . PRO   B 156 ? 0.654 0.045 0.552 0.099  0.013  -0.112 155 PRO   BBB CG  
3258 C  CD  . PRO   B 156 ? 0.511 0.026 0.473 0.083  0.020  -0.051 155 PRO   BBB CD  
3259 N  N   . LYS   B 157 ? 0.425 0.049 0.403 0.075  -0.037 -0.050 156 LYS   BBB N   
3260 C  CA  . LYS   B 157 ? 0.430 0.046 0.479 0.122  0.023  -0.042 156 LYS   BBB CA  
3261 C  C   . LYS   B 157 ? 0.384 0.079 0.385 0.029  -0.015 -0.029 156 LYS   BBB C   
3262 O  O   . LYS   B 157 ? 0.420 0.060 0.430 0.073  0.012  0.014  156 LYS   BBB O   
3263 C  CB  . LYS   B 157 ? 0.458 0.116 0.461 -0.033 -0.033 -0.038 156 LYS   BBB CB  
3264 C  CG  . LYS   B 157 ? 0.538 0.283 0.526 -0.024 0.004  -0.120 156 LYS   BBB CG  
3265 C  CD  . LYS   B 157 ? 0.530 0.311 0.608 -0.055 0.030  -0.148 156 LYS   BBB CD  
3266 C  CE  . LYS   B 157 ? 0.670 0.516 0.625 -0.032 -0.053 -0.173 156 LYS   BBB CE  
3267 N  NZ  . LYS   B 157 ? 0.549 0.558 0.655 -0.017 0.026  -0.268 156 LYS   BBB NZ  
3268 N  N   . LEU   B 158 ? 0.327 0.127 0.426 0.044  0.009  -0.061 157 LEU   BBB N   
3269 C  CA  . LEU   B 158 ? 0.346 0.035 0.432 -0.003 0.014  -0.023 157 LEU   BBB CA  
3270 C  C   . LEU   B 158 ? 0.389 0.152 0.400 0.099  -0.029 -0.108 157 LEU   BBB C   
3271 O  O   . LEU   B 158 ? 0.347 0.069 0.416 0.066  -0.001 -0.078 157 LEU   BBB O   
3272 C  CB  . LEU   B 158 ? 0.338 0.076 0.442 -0.041 -0.032 -0.001 157 LEU   BBB CB  
3273 C  CG  . LEU   B 158 ? 0.325 0.072 0.406 -0.001 -0.008 -0.010 157 LEU   BBB CG  
3274 C  CD1 . LEU   B 158 ? 0.360 0.103 0.458 -0.029 -0.008 -0.069 157 LEU   BBB CD1 
3275 C  CD2 . LEU   B 158 ? 0.351 0.047 0.546 -0.055 0.005  0.021  157 LEU   BBB CD2 
3276 N  N   . GLN   B 159 ? 0.486 0.164 0.481 0.164  -0.004 -0.059 158 GLN   BBB N   
3277 C  CA  . GLN   B 159 ? 0.459 0.341 0.469 0.209  -0.005 -0.083 158 GLN   BBB CA  
3278 C  C   . GLN   B 159 ? 0.448 0.183 0.425 0.155  -0.034 -0.093 158 GLN   BBB C   
3279 O  O   . GLN   B 159 ? 0.461 0.180 0.445 0.097  -0.036 -0.078 158 GLN   BBB O   
3280 C  CB  . GLN   B 159 ? 0.659 0.294 0.526 0.352  -0.001 0.047  158 GLN   BBB CB  
3281 C  CG  . GLN   B 159 ? 0.541 0.592 0.426 0.271  -0.017 -0.011 158 GLN   BBB CG  
3282 C  CD  . GLN   B 159 ? 0.530 0.888 0.591 0.134  -0.015 0.096  158 GLN   BBB CD  
3283 O  OE1 . GLN   B 159 ? 0.708 1.373 0.658 -0.233 0.025  0.085  158 GLN   BBB OE1 
3284 N  NE2 . GLN   B 159 ? 0.525 1.084 0.583 0.071  -0.059 0.163  158 GLN   BBB NE2 
3285 N  N   . LYS   B 160 ? 0.485 0.052 0.395 0.148  -0.022 -0.018 159 LYS   BBB N   
3286 C  CA  . LYS   B 160 ? 0.420 0.175 0.398 0.117  -0.031 -0.082 159 LYS   BBB CA  
3287 C  C   . LYS   B 160 ? 0.411 0.034 0.389 0.087  -0.051 -0.001 159 LYS   BBB C   
3288 O  O   . LYS   B 160 ? 0.386 0.112 0.434 0.040  -0.053 -0.010 159 LYS   BBB O   
3289 C  CB  . LYS   B 160 ? 0.572 0.075 0.592 0.026  -0.029 -0.040 159 LYS   BBB CB  
3290 C  CG  . LYS   B 160 ? 0.587 0.244 0.537 0.046  -0.091 0.041  159 LYS   BBB CG  
3291 C  CD  . LYS   B 160 ? 0.584 0.285 0.570 0.032  -0.029 0.034  159 LYS   BBB CD  
3292 C  CE  . LYS   B 160 ? 0.701 0.052 0.517 0.097  -0.034 0.015  159 LYS   BBB CE  
3293 N  NZ  . LYS   B 160 ? 0.914 0.173 0.640 0.321  -0.074 0.093  159 LYS   BBB NZ  
3294 N  N   . VAL   B 161 ? 0.404 0.054 0.386 0.091  -0.016 0.024  160 VAL   BBB N   
3295 C  CA  . VAL   B 161 ? 0.331 0.095 0.444 0.068  0.003  -0.013 160 VAL   BBB CA  
3296 C  C   . VAL   B 161 ? 0.309 0.040 0.398 0.084  -0.001 0.046  160 VAL   BBB C   
3297 O  O   . VAL   B 161 ? 0.423 0.009 0.431 0.035  0.025  -0.000 160 VAL   BBB O   
3298 C  CB  . VAL   B 161 ? 0.365 0.097 0.407 0.079  -0.012 -0.045 160 VAL   BBB CB  
3299 C  CG1 . VAL   B 161 ? 0.497 0.047 0.560 0.119  -0.028 0.072  160 VAL   BBB CG1 
3300 C  CG2 . VAL   B 161 ? 0.375 0.039 0.550 0.019  -0.026 -0.044 160 VAL   BBB CG2 
3301 N  N   . LEU   B 162 ? 0.351 0.008 0.399 0.018  0.043  -0.009 161 LEU   BBB N   
3302 C  CA  . LEU   B 162 ? 0.399 0.202 0.383 -0.054 0.007  -0.014 161 LEU   BBB CA  
3303 C  C   . LEU   B 162 ? 0.399 0.048 0.380 -0.028 0.039  -0.048 161 LEU   BBB C   
3304 O  O   . LEU   B 162 ? 0.383 0.098 0.409 -0.010 0.017  -0.058 161 LEU   BBB O   
3305 C  CB  . LEU   B 162 ? 0.455 0.325 0.349 -0.037 0.020  0.046  161 LEU   BBB CB  
3306 C  CG  . LEU   B 162 ? 0.452 0.033 0.477 -0.109 -0.016 -0.003 161 LEU   BBB CG  
3307 C  CD1 . LEU   B 162 ? 0.490 0.285 0.536 -0.125 0.023  0.018  161 LEU   BBB CD1 
3308 C  CD2 . LEU   B 162 ? 0.539 0.023 0.570 -0.090 -0.025 -0.024 161 LEU   BBB CD2 
3309 N  N   . ASP   B 163 ? 0.355 0.047 0.399 0.032  0.017  -0.029 162 ASP   BBB N   
3310 C  CA  . ASP   B 163 ? 0.357 0.049 0.480 0.093  -0.002 -0.027 162 ASP   BBB CA  
3311 C  C   . ASP   B 163 ? 0.339 0.079 0.396 0.081  -0.045 -0.033 162 ASP   BBB C   
3312 O  O   . ASP   B 163 ? 0.385 0.174 0.412 0.080  -0.034 0.018  162 ASP   BBB O   
3313 C  CB  . ASP   B 163 ? 0.405 0.028 0.455 0.028  -0.022 -0.049 162 ASP   BBB CB  
3314 C  CG  . ASP   B 163 ? 0.410 0.141 0.504 0.078  0.003  -0.069 162 ASP   BBB CG  
3315 O  OD1 . ASP   B 163 ? 0.392 0.200 0.612 0.087  0.048  -0.066 162 ASP   BBB OD1 
3316 O  OD2 . ASP   B 163 ? 0.562 0.187 0.597 0.130  0.031  -0.128 162 ASP   BBB OD2 
3317 N  N   . ALA   B 164 ? 0.313 0.016 0.428 0.047  0.010  -0.031 163 ALA   BBB N   
3318 C  CA  . ALA   B 164 ? 0.358 0.025 0.406 0.054  0.004  -0.007 163 ALA   BBB CA  
3319 C  C   . ALA   B 164 ? 0.319 0.081 0.418 0.050  0.009  -0.050 163 ALA   BBB C   
3320 O  O   . ALA   B 164 ? 0.386 0.039 0.465 0.103  -0.007 -0.047 163 ALA   BBB O   
3321 C  CB  . ALA   B 164 ? 0.382 0.021 0.433 0.048  -0.034 -0.037 163 ALA   BBB CB  
3322 N  N   . LEU   B 165 ? 0.327 0.112 0.375 0.033  0.021  -0.029 164 LEU   BBB N   
3323 C  CA  . LEU   B 165 ? 0.283 0.131 0.368 0.053  -0.008 -0.049 164 LEU   BBB CA  
3324 C  C   . LEU   B 165 ? 0.252 0.133 0.358 0.065  0.003  -0.018 164 LEU   BBB C   
3325 O  O   . LEU   B 165 ? 0.347 0.084 0.394 0.050  0.003  -0.045 164 LEU   BBB O   
3326 C  CB  . LEU   B 165 ? 0.356 0.087 0.383 0.011  -0.009 -0.071 164 LEU   BBB CB  
3327 C  CG  . LEU   B 165 ? 0.338 0.086 0.395 -0.013 -0.010 -0.061 164 LEU   BBB CG  
3328 C  CD1 . LEU   B 165 ? 0.381 0.023 0.475 0.078  -0.032 0.005  164 LEU   BBB CD1 
3329 C  CD2 . LEU   B 165 ? 0.340 0.132 0.398 0.071  -0.059 -0.018 164 LEU   BBB CD2 
3330 N  N   . GLN   B 166 ? 0.280 0.087 0.415 0.066  -0.025 -0.005 165 GLN   BBB N   
3331 C  CA  . GLN   B 166 ? 0.322 0.099 0.407 0.073  -0.023 0.005  165 GLN   BBB CA  
3332 C  C   . GLN   B 166 ? 0.319 0.068 0.386 0.082  -0.040 0.004  165 GLN   BBB C   
3333 O  O   . GLN   B 166 ? 0.345 0.192 0.403 0.072  -0.044 -0.016 165 GLN   BBB O   
3334 C  CB  . GLN   B 166 ? 0.373 0.184 0.447 0.130  -0.048 -0.041 165 GLN   BBB CB  
3335 C  CG  . GLN   B 166 ? 0.364 0.172 0.521 0.073  -0.006 -0.021 165 GLN   BBB CG  
3336 C  CD  . GLN   B 166 ? 0.429 0.314 0.528 0.029  0.063  0.009  165 GLN   BBB CD  
3337 O  OE1 . GLN   B 166 ? 0.455 0.007 0.579 0.018  -0.013 -0.005 165 GLN   BBB OE1 
3338 N  NE2 . GLN   B 166 ? 0.418 0.383 0.487 0.064  0.016  0.027  165 GLN   BBB NE2 
3339 N  N   . ALA   B 167 ? 0.333 0.139 0.406 0.081  -0.001 0.005  166 ALA   BBB N   
3340 C  CA  . ALA   B 167 ? 0.326 0.090 0.404 0.011  -0.003 -0.017 166 ALA   BBB CA  
3341 C  C   . ALA   B 167 ? 0.375 0.152 0.316 0.057  -0.008 -0.039 166 ALA   BBB C   
3342 O  O   . ALA   B 167 ? 0.345 0.075 0.391 0.042  -0.013 -0.020 166 ALA   BBB O   
3343 C  CB  . ALA   B 167 ? 0.360 0.100 0.427 -0.019 -0.000 -0.010 166 ALA   BBB CB  
3344 N  N   . ILE   B 168 ? 0.283 0.175 0.393 0.053  -0.007 -0.012 167 ILE   BBB N   
3345 C  CA  . ILE   B 168 ? 0.294 0.066 0.392 0.013  -0.012 -0.036 167 ILE   BBB CA  
3346 C  C   . ILE   B 168 ? 0.250 0.090 0.365 0.010  -0.055 -0.017 167 ILE   BBB C   
3347 O  O   . ILE   B 168 ? 0.267 0.107 0.392 0.020  -0.029 0.021  167 ILE   BBB O   
3348 C  CB  . ILE   B 168 ? 0.316 0.052 0.392 -0.019 -0.013 -0.031 167 ILE   BBB CB  
3349 C  CG1 . ILE   B 168 ? 0.313 0.051 0.397 0.018  -0.024 -0.028 167 ILE   BBB CG1 
3350 C  CG2 . ILE   B 168 ? 0.319 0.016 0.462 0.043  0.007  -0.042 167 ILE   BBB CG2 
3351 C  CD1 . ILE   B 168 ? 0.314 0.022 0.463 0.005  -0.044 -0.010 167 ILE   BBB CD1 
3352 N  N   . LYS   B 169 ? 0.259 0.068 0.409 0.043  -0.043 -0.012 168 LYS   BBB N   
3353 C  CA  . LYS   B 169 ? 0.269 0.149 0.383 -0.009 0.017  -0.018 168 LYS   BBB CA  
3354 C  C   . LYS   B 169 ? 0.288 0.149 0.375 0.037  0.029  0.029  168 LYS   BBB C   
3355 O  O   . LYS   B 169 ? 0.311 0.108 0.369 0.014  0.012  -0.005 168 LYS   BBB O   
3356 C  CB  . LYS   B 169 ? 0.302 0.172 0.465 0.049  -0.014 0.023  168 LYS   BBB CB  
3357 C  CG  . LYS   B 169 ? 0.323 0.382 0.507 -0.046 0.039  0.023  168 LYS   BBB CG  
3358 C  CD  . LYS   B 169 ? 0.421 0.550 0.478 -0.080 0.018  0.095  168 LYS   BBB CD  
3359 C  CE  . LYS   B 169 ? 0.477 0.599 0.711 -0.125 0.099  0.079  168 LYS   BBB CE  
3360 N  NZ  . LYS   B 169 ? 0.740 0.494 0.793 -0.310 -0.062 0.139  168 LYS   BBB NZ  
3361 N  N   . THR   B 170 ? 0.290 0.070 0.356 0.043  0.011  -0.016 169 THR   BBB N   
3362 C  CA  . THR   B 170 ? 0.287 0.093 0.396 0.026  0.013  -0.057 169 THR   BBB CA  
3363 C  C   . THR   B 170 ? 0.302 0.143 0.414 0.018  -0.034 -0.079 169 THR   BBB C   
3364 O  O   . THR   B 170 ? 0.281 0.110 0.407 0.019  -0.025 -0.018 169 THR   BBB O   
3365 C  CB  . THR   B 170 ? 0.306 0.146 0.370 0.033  0.039  -0.054 169 THR   BBB CB  
3366 O  OG1 . THR   B 170 ? 0.293 0.218 0.358 -0.023 0.020  0.008  169 THR   BBB OG1 
3367 C  CG2 . THR   B 170 ? 0.298 0.198 0.423 0.030  0.002  -0.035 169 THR   BBB CG2 
3368 N  N   . LYS   B 171 ? 0.287 0.101 0.397 -0.018 0.013  -0.057 170 LYS   BBB N   
3369 C  CA  . LYS   B 171 ? 0.285 0.091 0.415 0.005  0.016  -0.087 170 LYS   BBB CA  
3370 C  C   . LYS   B 171 ? 0.279 0.151 0.366 0.026  -0.022 -0.029 170 LYS   BBB C   
3371 O  O   . LYS   B 171 ? 0.305 0.143 0.373 0.020  0.017  -0.017 170 LYS   BBB O   
3372 C  CB  . LYS   B 171 ? 0.328 0.106 0.440 0.037  0.027  -0.090 170 LYS   BBB CB  
3373 C  CG  . LYS   B 171 ? 0.343 0.080 0.465 0.025  0.007  -0.032 170 LYS   BBB CG  
3374 C  CD  . LYS   B 171 ? 0.407 0.096 0.513 0.035  0.040  -0.070 170 LYS   BBB CD  
3375 C  CE  . LYS   B 171 ? 0.478 0.245 0.566 0.152  0.026  -0.102 170 LYS   BBB CE  
3376 N  NZ  . LYS   B 171 ? 0.749 0.249 0.721 0.143  0.004  -0.017 170 LYS   BBB NZ  
3377 N  N   . GLY   B 172 ? 0.266 0.136 0.367 0.028  -0.003 -0.043 171 GLY   BBB N   
3378 C  CA  . GLY   B 172 ? 0.270 0.162 0.413 0.028  0.043  -0.078 171 GLY   BBB CA  
3379 C  C   . GLY   B 172 ? 0.261 0.131 0.416 0.004  0.076  -0.040 171 GLY   BBB C   
3380 O  O   . GLY   B 172 ? 0.312 0.138 0.461 -0.021 0.045  -0.015 171 GLY   BBB O   
3381 N  N   . LYS   B 173 ? 0.253 0.027 0.406 -0.006 0.032  -0.031 172 LYS   BBB N   
3382 C  CA  . LYS   B 173 ? 0.305 0.061 0.396 0.048  0.029  -0.039 172 LYS   BBB CA  
3383 C  C   . LYS   B 173 ? 0.315 0.033 0.364 -0.025 0.012  0.033  172 LYS   BBB C   
3384 O  O   . LYS   B 173 ? 0.335 0.007 0.383 -0.018 -0.008 -0.004 172 LYS   BBB O   
3385 C  CB  . LYS   B 173 ? 0.289 0.014 0.426 0.046  -0.005 -0.008 172 LYS   BBB CB  
3386 C  CG  . LYS   B 173 ? 0.390 0.144 0.462 0.080  -0.030 -0.102 172 LYS   BBB CG  
3387 C  CD  . LYS   B 173 ? 0.382 0.366 0.472 0.093  -0.032 -0.032 172 LYS   BBB CD  
3388 C  CE  . LYS   B 173 ? 0.414 0.359 0.528 0.063  -0.093 -0.078 172 LYS   BBB CE  
3389 N  NZ  . LYS   B 173 ? 0.416 0.433 0.514 0.069  -0.034 0.017  172 LYS   BBB NZ  
3390 N  N   . ARG   B 174 ? 0.361 0.021 0.380 0.005  -0.016 0.033  173 ARG   BBB N   
3391 C  CA  A ARG   B 174 ? 0.333 0.043 0.355 0.104  -0.037 0.021  173 ARG   BBB CA  
3392 C  CA  B ARG   B 174 ? 0.326 0.035 0.338 0.093  -0.018 0.018  173 ARG   BBB CA  
3393 C  C   . ARG   B 174 ? 0.330 0.028 0.365 0.079  -0.011 0.026  173 ARG   BBB C   
3394 O  O   . ARG   B 174 ? 0.372 0.061 0.423 0.080  -0.050 0.034  173 ARG   BBB O   
3395 C  CB  A ARG   B 174 ? 0.314 0.106 0.421 0.163  -0.048 0.048  173 ARG   BBB CB  
3396 C  CB  B ARG   B 174 ? 0.317 0.057 0.348 0.065  -0.015 0.008  173 ARG   BBB CB  
3397 C  CG  A ARG   B 174 ? 0.350 0.262 0.441 0.082  -0.059 0.073  173 ARG   BBB CG  
3398 C  CG  B ARG   B 174 ? 0.346 0.056 0.323 0.050  -0.024 -0.010 173 ARG   BBB CG  
3399 C  CD  A ARG   B 174 ? 0.348 0.412 0.514 0.126  -0.051 0.081  173 ARG   BBB CD  
3400 C  CD  B ARG   B 174 ? 0.271 0.062 0.343 -0.009 -0.059 -0.015 173 ARG   BBB CD  
3401 N  NE  A ARG   B 174 ? 0.257 0.498 0.613 0.072  -0.040 0.059  173 ARG   BBB NE  
3402 N  NE  B ARG   B 174 ? 0.304 0.038 0.383 0.023  -0.018 -0.016 173 ARG   BBB NE  
3403 C  CZ  A ARG   B 174 ? 0.442 0.302 0.464 0.125  -0.040 0.056  173 ARG   BBB CZ  
3404 C  CZ  B ARG   B 174 ? 0.288 0.086 0.397 0.038  -0.022 -0.063 173 ARG   BBB CZ  
3405 N  NH1 A ARG   B 174 ? 0.388 0.527 0.490 0.276  -0.052 0.041  173 ARG   BBB NH1 
3406 N  NH1 B ARG   B 174 ? 0.323 0.027 0.412 0.034  0.005  -0.016 173 ARG   BBB NH1 
3407 N  NH2 A ARG   B 174 ? 0.280 0.107 0.544 0.052  -0.006 0.077  173 ARG   BBB NH2 
3408 N  NH2 B ARG   B 174 ? 0.261 0.158 0.421 -0.002 0.000  -0.048 173 ARG   BBB NH2 
3409 N  N   . ALA   B 175 ? 0.373 0.017 0.374 0.051  -0.031 0.031  174 ALA   BBB N   
3410 C  CA  . ALA   B 175 ? 0.404 0.014 0.405 0.052  -0.007 0.023  174 ALA   BBB CA  
3411 C  C   . ALA   B 175 ? 0.431 0.050 0.410 -0.022 -0.026 0.088  174 ALA   BBB C   
3412 O  O   . ALA   B 175 ? 0.397 0.011 0.419 0.032  -0.014 0.029  174 ALA   BBB O   
3413 C  CB  . ALA   B 175 ? 0.381 0.039 0.430 0.110  -0.008 0.011  174 ALA   BBB CB  
3414 N  N   . PRO   B 176 ? 0.370 0.036 0.437 0.008  -0.042 0.059  175 PRO   BBB N   
3415 C  CA  . PRO   B 176 ? 0.470 0.020 0.436 0.066  -0.060 0.032  175 PRO   BBB CA  
3416 C  C   . PRO   B 176 ? 0.408 0.012 0.500 0.012  -0.024 -0.003 175 PRO   BBB C   
3417 O  O   . PRO   B 176 ? 0.400 0.078 0.519 0.015  -0.023 0.016  175 PRO   BBB O   
3418 C  CB  . PRO   B 176 ? 0.542 0.012 0.503 0.042  -0.034 0.035  175 PRO   BBB CB  
3419 C  CG  . PRO   B 176 ? 0.541 0.043 0.507 -0.049 -0.074 0.076  175 PRO   BBB CG  
3420 C  CD  . PRO   B 176 ? 0.468 0.013 0.424 0.050  -0.068 0.008  175 PRO   BBB CD  
3421 N  N   . PHE   B 177 ? 0.384 0.010 0.450 0.036  0.009  0.005  176 PHE   BBB N   
3422 C  CA  . PHE   B 177 ? 0.490 0.017 0.474 0.069  -0.010 -0.022 176 PHE   BBB CA  
3423 C  C   . PHE   B 177 ? 0.415 0.007 0.435 0.013  0.023  -0.007 176 PHE   BBB C   
3424 O  O   . PHE   B 177 ? 0.444 0.067 0.610 0.027  -0.030 -0.021 176 PHE   BBB O   
3425 C  CB  . PHE   B 177 ? 0.409 0.008 0.440 0.021  0.001  0.016  176 PHE   BBB CB  
3426 C  CG  . PHE   B 177 ? 0.437 0.011 0.472 0.041  0.012  -0.013 176 PHE   BBB CG  
3427 C  CD1 . PHE   B 177 ? 0.486 0.014 0.432 0.046  -0.000 -0.039 176 PHE   BBB CD1 
3428 C  CD2 . PHE   B 177 ? 0.405 0.055 0.421 0.062  0.011  -0.003 176 PHE   BBB CD2 
3429 C  CE1 . PHE   B 177 ? 0.425 0.024 0.455 0.011  -0.001 -0.027 176 PHE   BBB CE1 
3430 C  CE2 . PHE   B 177 ? 0.443 0.091 0.433 0.032  0.022  0.034  176 PHE   BBB CE2 
3431 C  CZ  . PHE   B 177 ? 0.413 0.018 0.408 0.025  0.022  0.017  176 PHE   BBB CZ  
3432 N  N   . THR   B 178 ? 0.520 0.022 0.523 0.045  -0.016 -0.003 177 THR   BBB N   
3433 C  CA  . THR   B 178 ? 0.492 0.040 0.429 -0.039 0.032  0.110  177 THR   BBB CA  
3434 C  C   . THR   B 178 ? 0.507 0.138 0.440 0.090  -0.016 0.106  177 THR   BBB C   
3435 O  O   . THR   B 178 ? 0.490 0.149 0.494 0.097  0.045  -0.035 177 THR   BBB O   
3436 C  CB  . THR   B 178 ? 0.545 0.052 0.482 -0.139 0.026  0.064  177 THR   BBB CB  
3437 O  OG1 . THR   B 178 ? 0.599 0.087 0.489 -0.009 -0.019 0.046  177 THR   BBB OG1 
3438 C  CG2 . THR   B 178 ? 0.671 0.045 0.489 -0.061 0.068  0.119  177 THR   BBB CG2 
3439 N  N   . ASN   B 179 ? 0.687 0.096 0.473 0.116  -0.030 0.062  178 ASN   BBB N   
3440 C  CA  . ASN   B 179 ? 0.638 0.047 0.490 0.122  0.010  0.046  178 ASN   BBB CA  
3441 C  C   . ASN   B 179 ? 0.521 0.192 0.483 0.064  -0.057 0.084  178 ASN   BBB C   
3442 O  O   . ASN   B 179 ? 0.568 0.018 0.516 0.045  0.038  -0.030 178 ASN   BBB O   
3443 C  CB  . ASN   B 179 ? 0.587 0.096 0.467 0.140  -0.010 0.031  178 ASN   BBB CB  
3444 C  CG  . ASN   B 179 ? 0.680 0.166 0.504 0.079  -0.068 -0.016 178 ASN   BBB CG  
3445 O  OD1 . ASN   B 179 ? 0.778 0.342 0.671 0.015  0.126  -0.199 178 ASN   BBB OD1 
3446 N  ND2 . ASN   B 179 ? 0.688 0.203 0.606 0.125  -0.138 -0.042 178 ASN   BBB ND2 
3447 N  N   . PHE   B 180 ? 0.510 0.038 0.470 0.043  -0.007 0.024  179 PHE   BBB N   
3448 C  CA  . PHE   B 180 ? 0.591 0.165 0.496 -0.085 -0.024 0.023  179 PHE   BBB CA  
3449 C  C   . PHE   B 180 ? 0.558 0.013 0.576 -0.055 -0.035 -0.026 179 PHE   BBB C   
3450 O  O   . PHE   B 180 ? 0.474 0.023 0.470 -0.080 -0.024 0.039  179 PHE   BBB O   
3451 C  CB  . PHE   B 180 ? 0.508 0.014 0.547 0.050  0.021  0.041  179 PHE   BBB CB  
3452 C  CG  . PHE   B 180 ? 0.553 0.011 0.455 0.034  0.008  0.032  179 PHE   BBB CG  
3453 C  CD1 . PHE   B 180 ? 0.514 0.029 0.602 -0.017 -0.009 -0.011 179 PHE   BBB CD1 
3454 C  CD2 . PHE   B 180 ? 0.476 0.031 0.463 0.107  0.022  0.007  179 PHE   BBB CD2 
3455 C  CE1 . PHE   B 180 ? 0.502 0.045 0.591 0.121  0.020  0.078  179 PHE   BBB CE1 
3456 C  CE2 . PHE   B 180 ? 0.507 0.019 0.418 0.078  -0.013 -0.019 179 PHE   BBB CE2 
3457 C  CZ  . PHE   B 180 ? 0.462 0.023 0.474 0.001  0.005  0.089  179 PHE   BBB CZ  
3458 N  N   . ASP   B 181 ? 0.674 0.034 0.659 0.043  0.037  0.053  180 ASP   BBB N   
3459 C  CA  . ASP   B 181 ? 0.714 0.093 0.399 -0.121 0.047  0.024  180 ASP   BBB CA  
3460 C  C   . ASP   B 181 ? 0.526 0.040 0.379 0.012  -0.040 -0.009 180 ASP   BBB C   
3461 O  O   . ASP   B 181 ? 0.563 0.074 0.462 -0.003 -0.007 -0.043 180 ASP   BBB O   
3462 C  CB  . ASP   B 181 ? 0.707 0.138 0.366 -0.104 -0.062 0.023  180 ASP   BBB CB  
3463 C  CG  . ASP   B 181 ? 0.697 0.112 0.374 0.031  -0.016 0.023  180 ASP   BBB CG  
3464 O  OD1 . ASP   B 181 ? 0.555 0.084 0.525 -0.017 -0.082 0.009  180 ASP   BBB OD1 
3465 O  OD2 . ASP   B 181 ? 0.825 0.233 0.444 0.000  0.052  -0.047 180 ASP   BBB OD2 
3466 N  N   . PRO   B 182 ? 0.533 0.013 0.460 -0.054 0.019  -0.028 181 PRO   BBB N   
3467 C  CA  . PRO   B 182 ? 0.518 0.020 0.414 -0.082 0.001  -0.014 181 PRO   BBB CA  
3468 C  C   . PRO   B 182 ? 0.480 0.110 0.371 -0.083 0.040  -0.047 181 PRO   BBB C   
3469 O  O   . PRO   B 182 ? 0.510 0.007 0.451 0.000  -0.003 0.023  181 PRO   BBB O   
3470 C  CB  . PRO   B 182 ? 0.594 0.085 0.461 -0.005 0.036  -0.037 181 PRO   BBB CB  
3471 C  CG  . PRO   B 182 ? 0.622 0.007 0.503 0.008  0.018  -0.006 181 PRO   BBB CG  
3472 C  CD  . PRO   B 182 ? 0.577 0.012 0.547 -0.057 0.084  0.004  181 PRO   BBB CD  
3473 N  N   . SER   B 183 ? 0.444 0.018 0.435 -0.067 -0.001 -0.021 182 SER   BBB N   
3474 C  CA  . SER   B 183 ? 0.468 0.017 0.428 -0.069 0.000  0.015  182 SER   BBB CA  
3475 C  C   . SER   B 183 ? 0.431 0.091 0.340 -0.049 -0.055 -0.060 182 SER   BBB C   
3476 O  O   . SER   B 183 ? 0.410 0.008 0.415 0.016  -0.037 -0.022 182 SER   BBB O   
3477 C  CB  . SER   B 183 ? 0.436 0.117 0.432 -0.018 -0.035 -0.032 182 SER   BBB CB  
3478 O  OG  . SER   B 183 ? 0.526 0.094 0.455 -0.054 0.070  -0.069 182 SER   BBB OG  
3479 N  N   . THR   B 184 ? 0.431 0.014 0.408 -0.057 -0.020 0.013  183 THR   BBB N   
3480 C  CA  . THR   B 184 ? 0.422 0.028 0.387 -0.094 -0.045 -0.006 183 THR   BBB CA  
3481 C  C   . THR   B 184 ? 0.415 0.015 0.396 -0.046 -0.030 -0.033 183 THR   BBB C   
3482 O  O   . THR   B 184 ? 0.487 0.008 0.514 0.025  0.038  -0.009 183 THR   BBB O   
3483 C  CB  . THR   B 184 ? 0.540 0.034 0.441 -0.042 -0.042 0.047  183 THR   BBB CB  
3484 O  OG1 . THR   B 184 ? 0.528 0.017 0.435 0.025  -0.059 0.006  183 THR   BBB OG1 
3485 C  CG2 . THR   B 184 ? 0.530 0.082 0.480 -0.066 0.024  -0.029 183 THR   BBB CG2 
3486 N  N   . LEU   B 185 ? 0.378 0.012 0.391 -0.042 0.005  -0.013 184 LEU   BBB N   
3487 C  CA  . LEU   B 185 ? 0.379 0.015 0.408 -0.053 -0.033 0.025  184 LEU   BBB CA  
3488 C  C   . LEU   B 185 ? 0.317 0.019 0.396 -0.062 -0.028 0.013  184 LEU   BBB C   
3489 O  O   . LEU   B 185 ? 0.387 0.009 0.489 -0.023 -0.037 -0.018 184 LEU   BBB O   
3490 C  CB  . LEU   B 185 ? 0.354 0.007 0.416 -0.017 -0.020 0.006  184 LEU   BBB CB  
3491 C  CG  . LEU   B 185 ? 0.411 0.011 0.425 -0.041 -0.055 0.015  184 LEU   BBB CG  
3492 C  CD1 . LEU   B 185 ? 0.558 0.010 0.500 -0.034 -0.046 -0.022 184 LEU   BBB CD1 
3493 C  CD2 . LEU   B 185 ? 0.419 0.021 0.529 -0.007 -0.027 0.009  184 LEU   BBB CD2 
3494 N  N   . LEU   B 186 ? 0.322 0.009 0.439 -0.027 -0.040 -0.002 185 LEU   BBB N   
3495 C  CA  . LEU   B 186 ? 0.367 0.012 0.405 0.022  -0.058 -0.043 185 LEU   BBB CA  
3496 C  C   . LEU   B 186 ? 0.346 0.020 0.417 0.065  -0.028 -0.026 185 LEU   BBB C   
3497 O  O   . LEU   B 186 ? 0.396 0.009 0.487 0.031  -0.032 -0.014 185 LEU   BBB O   
3498 C  CB  . LEU   B 186 ? 0.376 0.014 0.476 0.053  -0.065 0.001  185 LEU   BBB CB  
3499 C  CG  . LEU   B 186 ? 0.414 0.017 0.583 0.067  -0.001 -0.005 185 LEU   BBB CG  
3500 C  CD1 . LEU   B 186 ? 0.445 0.031 0.534 0.093  -0.066 -0.066 185 LEU   BBB CD1 
3501 C  CD2 . LEU   B 186 ? 0.379 0.012 0.651 0.039  -0.016 -0.038 185 LEU   BBB CD2 
3502 N  N   . PRO   B 187 ? 0.474 0.016 0.523 -0.008 -0.044 -0.068 186 PRO   BBB N   
3503 C  CA  . PRO   B 187 ? 0.439 0.009 0.535 -0.009 -0.059 -0.035 186 PRO   BBB CA  
3504 C  C   . PRO   B 187 ? 0.440 0.011 0.463 -0.039 -0.087 -0.014 186 PRO   BBB C   
3505 O  O   . PRO   B 187 ? 0.376 0.010 0.484 0.037  -0.021 -0.011 186 PRO   BBB O   
3506 C  CB  . PRO   B 187 ? 0.387 0.027 0.463 -0.065 -0.007 0.066  186 PRO   BBB CB  
3507 C  CG  . PRO   B 187 ? 0.383 0.013 0.488 -0.032 -0.012 -0.044 186 PRO   BBB CG  
3508 C  CD  . PRO   B 187 ? 0.393 0.015 0.508 0.007  -0.018 -0.065 186 PRO   BBB CD  
3509 N  N   . SER   B 188 ? 0.529 0.007 0.554 -0.019 -0.064 -0.013 187 SER   BBB N   
3510 C  CA  A SER   B 188 ? 0.456 0.016 0.475 -0.035 -0.062 -0.052 187 SER   BBB CA  
3511 C  CA  B SER   B 188 ? 0.429 0.016 0.468 -0.024 -0.046 -0.058 187 SER   BBB CA  
3512 C  C   . SER   B 188 ? 0.408 0.012 0.419 -0.047 -0.018 -0.005 187 SER   BBB C   
3513 O  O   . SER   B 188 ? 0.365 0.018 0.483 -0.025 -0.013 -0.003 187 SER   BBB O   
3514 C  CB  A SER   B 188 ? 0.497 0.019 0.485 -0.071 -0.019 -0.032 187 SER   BBB CB  
3515 C  CB  B SER   B 188 ? 0.397 0.013 0.469 -0.027 -0.049 -0.044 187 SER   BBB CB  
3516 O  OG  A SER   B 188 ? 0.506 0.223 0.464 -0.121 -0.059 0.002  187 SER   BBB OG  
3517 O  OG  B SER   B 188 ? 0.401 0.026 0.461 -0.044 -0.020 -0.079 187 SER   BBB OG  
3518 N  N   . SER   B 189 ? 0.444 0.012 0.494 0.019  -0.066 -0.051 188 SER   BBB N   
3519 C  CA  . SER   B 189 ? 0.392 0.133 0.404 -0.007 -0.064 -0.080 188 SER   BBB CA  
3520 C  C   . SER   B 189 ? 0.381 0.111 0.395 0.050  -0.071 -0.016 188 SER   BBB C   
3521 O  O   . SER   B 189 ? 0.358 0.095 0.427 0.020  -0.049 -0.017 188 SER   BBB O   
3522 C  CB  . SER   B 189 ? 0.468 0.190 0.445 -0.004 -0.041 -0.043 188 SER   BBB CB  
3523 O  OG  . SER   B 189 ? 0.471 0.198 0.565 -0.009 -0.076 -0.016 188 SER   BBB OG  
3524 N  N   . LEU   B 190 ? 0.402 0.012 0.507 0.039  -0.072 -0.035 189 LEU   BBB N   
3525 C  CA  . LEU   B 190 ? 0.339 0.176 0.424 0.011  -0.068 -0.017 189 LEU   BBB CA  
3526 C  C   . LEU   B 190 ? 0.368 0.102 0.386 0.011  -0.037 -0.022 189 LEU   BBB C   
3527 O  O   . LEU   B 190 ? 0.337 0.032 0.497 -0.001 -0.033 0.027  189 LEU   BBB O   
3528 C  CB  . LEU   B 190 ? 0.418 0.099 0.455 0.066  -0.080 0.010  189 LEU   BBB CB  
3529 C  CG  . LEU   B 190 ? 0.376 0.030 0.512 0.018  -0.071 0.027  189 LEU   BBB CG  
3530 C  CD1 . LEU   B 190 ? 0.425 0.218 0.474 -0.013 -0.025 0.044  189 LEU   BBB CD1 
3531 C  CD2 . LEU   B 190 ? 0.341 0.243 0.506 0.003  -0.078 0.015  189 LEU   BBB CD2 
3532 N  N   . ASP   B 191 ? 0.369 0.042 0.422 -0.002 -0.036 0.005  190 ASP   BBB N   
3533 C  CA  . ASP   B 191 ? 0.386 0.043 0.427 0.022  -0.044 -0.025 190 ASP   BBB CA  
3534 C  C   . ASP   B 191 ? 0.312 0.062 0.368 0.007  -0.026 0.009  190 ASP   BBB C   
3535 O  O   . ASP   B 191 ? 0.371 0.011 0.403 -0.041 -0.048 0.014  190 ASP   BBB O   
3536 C  CB  . ASP   B 191 ? 0.406 0.238 0.416 0.045  -0.028 -0.018 190 ASP   BBB CB  
3537 C  CG  . ASP   B 191 ? 0.341 0.300 0.447 -0.012 -0.036 -0.069 190 ASP   BBB CG  
3538 O  OD1 . ASP   B 191 ? 0.386 0.171 0.513 -0.001 -0.074 -0.140 190 ASP   BBB OD1 
3539 O  OD2 . ASP   B 191 ? 0.466 0.255 0.526 -0.028 0.067  -0.102 190 ASP   BBB OD2 
3540 N  N   . PHE   B 192 ? 0.316 0.009 0.406 -0.029 -0.032 0.013  191 PHE   BBB N   
3541 C  CA  . PHE   B 192 ? 0.266 0.077 0.386 0.026  -0.019 0.016  191 PHE   BBB CA  
3542 C  C   . PHE   B 192 ? 0.320 0.008 0.357 -0.022 -0.060 -0.005 191 PHE   BBB C   
3543 O  O   . PHE   B 192 ? 0.330 0.009 0.389 0.021  -0.040 0.021  191 PHE   BBB O   
3544 C  CB  . PHE   B 192 ? 0.292 0.033 0.417 -0.001 -0.036 0.019  191 PHE   BBB CB  
3545 C  CG  . PHE   B 192 ? 0.274 0.009 0.426 -0.020 -0.016 0.023  191 PHE   BBB CG  
3546 C  CD1 . PHE   B 192 ? 0.332 0.023 0.422 -0.048 -0.018 -0.035 191 PHE   BBB CD1 
3547 C  CD2 . PHE   B 192 ? 0.254 0.008 0.435 0.003  -0.034 0.027  191 PHE   BBB CD2 
3548 C  CE1 . PHE   B 192 ? 0.325 0.019 0.447 -0.055 -0.030 0.040  191 PHE   BBB CE1 
3549 C  CE2 . PHE   B 192 ? 0.267 0.032 0.419 0.027  -0.064 0.041  191 PHE   BBB CE2 
3550 C  CZ  . PHE   B 192 ? 0.292 0.077 0.405 -0.052 -0.028 0.029  191 PHE   BBB CZ  
3551 N  N   . TRP   B 193 ? 0.300 0.027 0.349 0.020  -0.013 -0.022 192 TRP   BBB N   
3552 C  CA  . TRP   B 193 ? 0.324 0.007 0.382 0.015  -0.015 -0.002 192 TRP   BBB CA  
3553 C  C   . TRP   B 193 ? 0.279 0.034 0.379 0.025  -0.039 0.004  192 TRP   BBB C   
3554 O  O   . TRP   B 193 ? 0.325 0.036 0.369 0.005  -0.040 0.029  192 TRP   BBB O   
3555 C  CB  . TRP   B 193 ? 0.357 0.020 0.383 -0.009 -0.016 -0.007 192 TRP   BBB CB  
3556 C  CG  . TRP   B 193 ? 0.316 0.011 0.402 -0.029 -0.008 0.026  192 TRP   BBB CG  
3557 C  CD1 . TRP   B 193 ? 0.346 0.044 0.410 0.015  -0.014 0.009  192 TRP   BBB CD1 
3558 C  CD2 . TRP   B 193 ? 0.310 0.014 0.396 -0.004 -0.009 0.009  192 TRP   BBB CD2 
3559 N  NE1 . TRP   B 193 ? 0.346 0.018 0.441 -0.055 -0.017 0.040  192 TRP   BBB NE1 
3560 C  CE2 . TRP   B 193 ? 0.369 0.012 0.432 -0.009 -0.015 0.048  192 TRP   BBB CE2 
3561 C  CE3 . TRP   B 193 ? 0.339 0.007 0.399 0.014  0.002  0.007  192 TRP   BBB CE3 
3562 C  CZ2 . TRP   B 193 ? 0.377 0.032 0.506 -0.030 0.004  0.107  192 TRP   BBB CZ2 
3563 C  CZ3 . TRP   B 193 ? 0.319 0.009 0.471 0.026  -0.012 0.007  192 TRP   BBB CZ3 
3564 C  CH2 . TRP   B 193 ? 0.326 0.023 0.478 -0.038 -0.001 0.045  192 TRP   BBB CH2 
3565 N  N   . THR   B 194 ? 0.283 0.026 0.418 0.013  -0.019 0.080  193 THR   BBB N   
3566 C  CA  . THR   B 194 ? 0.330 0.010 0.413 -0.015 -0.002 0.036  193 THR   BBB CA  
3567 C  C   . THR   B 194 ? 0.316 0.010 0.359 -0.028 -0.039 0.022  193 THR   BBB C   
3568 O  O   . THR   B 194 ? 0.364 0.023 0.421 -0.035 -0.052 0.054  193 THR   BBB O   
3569 C  CB  . THR   B 194 ? 0.406 0.019 0.384 -0.037 -0.022 0.061  193 THR   BBB CB  
3570 O  OG1 . THR   B 194 ? 0.353 0.022 0.432 -0.030 -0.013 0.075  193 THR   BBB OG1 
3571 C  CG2 . THR   B 194 ? 0.354 0.039 0.397 -0.000 -0.018 0.030  193 THR   BBB CG2 
3572 N  N   . TYR   B 195 ? 0.336 0.013 0.385 0.023  -0.004 0.046  194 TYR   BBB N   
3573 C  CA  . TYR   B 195 ? 0.299 0.017 0.438 0.049  0.012  0.038  194 TYR   BBB CA  
3574 C  C   . TYR   B 195 ? 0.305 0.107 0.368 0.066  -0.029 0.038  194 TYR   BBB C   
3575 O  O   . TYR   B 195 ? 0.297 0.026 0.422 -0.004 -0.027 0.060  194 TYR   BBB O   
3576 C  CB  . TYR   B 195 ? 0.269 0.043 0.456 0.038  -0.019 0.108  194 TYR   BBB CB  
3577 C  CG  . TYR   B 195 ? 0.276 0.058 0.398 0.043  0.019  0.040  194 TYR   BBB CG  
3578 C  CD1 . TYR   B 195 ? 0.279 0.012 0.510 0.007  0.007  0.054  194 TYR   BBB CD1 
3579 C  CD2 . TYR   B 195 ? 0.336 0.029 0.437 0.071  0.037  0.065  194 TYR   BBB CD2 
3580 C  CE1 . TYR   B 195 ? 0.259 0.029 0.477 0.018  0.030  0.036  194 TYR   BBB CE1 
3581 C  CE2 . TYR   B 195 ? 0.300 0.011 0.464 0.018  0.015  0.042  194 TYR   BBB CE2 
3582 C  CZ  . TYR   B 195 ? 0.250 0.020 0.423 -0.001 0.011  0.074  194 TYR   BBB CZ  
3583 O  OH  . TYR   B 195 ? 0.317 0.013 0.447 -0.024 -0.036 0.047  194 TYR   BBB OH  
3584 N  N   . PRO   B 196 ? 0.301 0.021 0.475 0.026  -0.007 0.074  195 PRO   BBB N   
3585 C  CA  . PRO   B 196 ? 0.307 0.058 0.457 0.036  -0.005 0.048  195 PRO   BBB CA  
3586 C  C   . PRO   B 196 ? 0.330 0.034 0.443 -0.004 -0.012 0.110  195 PRO   BBB C   
3587 O  O   . PRO   B 196 ? 0.434 0.026 0.502 0.060  0.019  0.077  195 PRO   BBB O   
3588 C  CB  . PRO   B 196 ? 0.325 0.053 0.481 0.050  -0.007 0.055  195 PRO   BBB CB  
3589 C  CG  . PRO   B 196 ? 0.305 0.203 0.490 -0.012 0.023  0.094  195 PRO   BBB CG  
3590 C  CD  . PRO   B 196 ? 0.292 0.144 0.421 0.012  -0.026 0.099  195 PRO   BBB CD  
3591 N  N   . GLY   B 197 ? 0.344 0.016 0.404 0.026  0.011  0.057  196 GLY   BBB N   
3592 C  CA  . GLY   B 197 ? 0.362 0.035 0.405 0.099  -0.018 0.018  196 GLY   BBB CA  
3593 C  C   . GLY   B 197 ? 0.313 0.009 0.430 0.022  0.015  0.015  196 GLY   BBB C   
3594 O  O   . GLY   B 197 ? 0.322 0.067 0.502 0.008  -0.006 0.068  196 GLY   BBB O   
3595 N  N   . SER   B 198 ? 0.306 0.007 0.474 0.005  0.012  0.011  197 SER   BBB N   
3596 C  CA  . SER   B 198 ? 0.327 0.007 0.476 0.012  0.018  0.010  197 SER   BBB CA  
3597 C  C   . SER   B 198 ? 0.259 0.029 0.395 -0.021 0.007  0.054  197 SER   BBB C   
3598 O  O   . SER   B 198 ? 0.285 0.006 0.446 0.004  0.005  -0.004 197 SER   BBB O   
3599 C  CB  . SER   B 198 ? 0.381 0.013 0.472 0.048  0.037  0.019  197 SER   BBB CB  
3600 O  OG  . SER   B 198 ? 0.343 0.015 0.471 0.047  0.031  0.034  197 SER   BBB OG  
3601 N  N   . LEU   B 199 ? 0.276 0.009 0.403 -0.006 0.000  0.034  198 LEU   BBB N   
3602 C  CA  . LEU   B 199 ? 0.284 0.041 0.421 0.003  -0.024 0.033  198 LEU   BBB CA  
3603 C  C   . LEU   B 199 ? 0.266 0.016 0.395 0.050  0.015  0.011  198 LEU   BBB C   
3604 O  O   . LEU   B 199 ? 0.299 0.024 0.452 0.061  0.014  0.049  198 LEU   BBB O   
3605 C  CB  . LEU   B 199 ? 0.288 0.016 0.433 -0.008 -0.001 0.041  198 LEU   BBB CB  
3606 C  CG  . LEU   B 199 ? 0.308 0.024 0.466 -0.016 -0.012 0.088  198 LEU   BBB CG  
3607 C  CD1 . LEU   B 199 ? 0.455 0.037 0.532 0.011  0.026  0.127  198 LEU   BBB CD1 
3608 C  CD2 . LEU   B 199 ? 0.343 0.078 0.416 -0.013 0.000  0.034  198 LEU   BBB CD2 
3609 N  N   . THR   B 200 ? 0.249 0.007 0.405 0.002  0.014  0.010  199 THR   BBB N   
3610 C  CA  . THR   B 200 ? 0.254 0.010 0.444 0.019  -0.021 0.026  199 THR   BBB CA  
3611 C  C   . THR   B 200 ? 0.269 0.017 0.447 0.054  -0.001 -0.004 199 THR   BBB C   
3612 O  O   . THR   B 200 ? 0.337 0.008 0.463 0.005  0.014  -0.024 199 THR   BBB O   
3613 C  CB  . THR   B 200 ? 0.278 0.029 0.408 0.034  -0.012 0.064  199 THR   BBB CB  
3614 O  OG1 . THR   B 200 ? 0.349 0.008 0.464 0.002  0.010  0.026  199 THR   BBB OG1 
3615 C  CG2 . THR   B 200 ? 0.298 0.018 0.422 0.026  -0.003 0.009  199 THR   BBB CG2 
3616 N  N   . HIS   B 201 ? 0.410 0.007 0.477 -0.004 0.020  0.008  200 HIS   BBB N   
3617 C  CA  . HIS   B 201 ? 0.362 0.013 0.407 -0.010 0.031  0.049  200 HIS   BBB CA  
3618 C  C   . HIS   B 201 ? 0.292 0.009 0.383 0.020  0.000  0.015  200 HIS   BBB C   
3619 O  O   . HIS   B 201 ? 0.316 0.018 0.461 0.038  -0.013 -0.008 200 HIS   BBB O   
3620 C  CB  . HIS   B 201 ? 0.374 0.010 0.456 -0.025 0.001  -0.031 200 HIS   BBB CB  
3621 C  CG  . HIS   B 201 ? 0.315 0.018 0.431 -0.043 0.009  -0.049 200 HIS   BBB CG  
3622 N  ND1 . HIS   B 201 ? 0.377 0.064 0.498 0.013  0.055  0.005  200 HIS   BBB ND1 
3623 C  CD2 . HIS   B 201 ? 0.285 0.013 0.408 0.041  0.019  -0.008 200 HIS   BBB CD2 
3624 C  CE1 . HIS   B 201 ? 0.325 0.037 0.405 0.041  0.011  0.008  200 HIS   BBB CE1 
3625 N  NE2 . HIS   B 201 ? 0.411 0.022 0.455 0.079  0.029  -0.003 200 HIS   BBB NE2 
3626 N  N   . PRO   B 202 ? 0.318 0.040 0.407 0.047  0.005  0.011  201 PRO   BBB N   
3627 C  CA  . PRO   B 202 ? 0.318 0.032 0.451 0.058  0.025  0.008  201 PRO   BBB CA  
3628 C  C   . PRO   B 202 ? 0.349 0.077 0.465 -0.004 0.014  0.028  201 PRO   BBB C   
3629 O  O   . PRO   B 202 ? 0.375 0.062 0.442 0.001  0.022  0.012  201 PRO   BBB O   
3630 C  CB  . PRO   B 202 ? 0.298 0.156 0.428 0.052  0.049  -0.000 201 PRO   BBB CB  
3631 C  CG  . PRO   B 202 ? 0.304 0.214 0.442 0.003  0.037  -0.004 201 PRO   BBB CG  
3632 C  CD  . PRO   B 202 ? 0.308 0.133 0.402 0.012  0.012  0.030  201 PRO   BBB CD  
3633 N  N   . PRO   B 203 ? 0.348 0.009 0.428 0.029  0.057  0.009  202 PRO   BBB N   
3634 C  CA  . PRO   B 203 ? 0.361 0.008 0.460 0.021  0.025  -0.006 202 PRO   BBB CA  
3635 C  C   . PRO   B 203 ? 0.339 0.024 0.446 0.036  0.061  0.028  202 PRO   BBB C   
3636 O  O   . PRO   B 203 ? 0.321 0.020 0.548 0.064  0.068  0.026  202 PRO   BBB O   
3637 C  CB  . PRO   B 203 ? 0.390 0.159 0.448 0.011  0.050  0.077  202 PRO   BBB CB  
3638 C  CG  . PRO   B 203 ? 0.373 0.160 0.476 -0.023 0.023  0.039  202 PRO   BBB CG  
3639 C  CD  . PRO   B 203 ? 0.361 0.085 0.487 -0.084 0.051  0.065  202 PRO   BBB CD  
3640 N  N   . LEU   B 204 ? 0.410 0.042 0.471 0.076  0.067  0.032  203 LEU   BBB N   
3641 C  CA  . LEU   B 204 ? 0.404 0.009 0.442 -0.035 0.017  0.004  203 LEU   BBB CA  
3642 C  C   . LEU   B 204 ? 0.342 0.104 0.405 0.004  0.052  0.075  203 LEU   BBB C   
3643 O  O   . LEU   B 204 ? 0.378 0.044 0.445 0.075  0.022  0.035  203 LEU   BBB O   
3644 C  CB  . LEU   B 204 ? 0.357 0.009 0.531 0.005  0.052  -0.006 203 LEU   BBB CB  
3645 C  CG  . LEU   B 204 ? 0.408 0.007 0.546 -0.002 0.006  -0.024 203 LEU   BBB CG  
3646 C  CD1 . LEU   B 204 ? 0.544 0.011 0.667 -0.020 0.038  -0.052 203 LEU   BBB CD1 
3647 C  CD2 . LEU   B 204 ? 0.335 0.009 0.568 -0.023 0.008  0.019  203 LEU   BBB CD2 
3648 N  N   . TYR   B 205 ? 0.308 0.103 0.458 -0.002 0.025  0.074  204 TYR   BBB N   
3649 C  CA  . TYR   B 205 ? 0.283 0.100 0.424 -0.011 0.046  0.066  204 TYR   BBB CA  
3650 C  C   . TYR   B 205 ? 0.228 0.069 0.433 -0.058 0.012  0.057  204 TYR   BBB C   
3651 O  O   . TYR   B 205 ? 0.281 0.150 0.470 0.013  0.032  0.039  204 TYR   BBB O   
3652 C  CB  . TYR   B 205 ? 0.390 0.068 0.463 0.002  0.043  0.080  204 TYR   BBB CB  
3653 C  CG  . TYR   B 205 ? 0.408 0.098 0.466 0.017  0.074  0.019  204 TYR   BBB CG  
3654 C  CD1 . TYR   B 205 ? 0.515 0.277 0.494 0.157  0.138  0.061  204 TYR   BBB CD1 
3655 C  CD2 . TYR   B 205 ? 0.396 0.280 0.549 0.020  -0.033 0.132  204 TYR   BBB CD2 
3656 C  CE1 . TYR   B 205 ? 0.528 0.415 0.493 0.135  0.100  0.062  204 TYR   BBB CE1 
3657 C  CE2 . TYR   B 205 ? 0.476 0.253 0.563 -0.020 0.060  0.045  204 TYR   BBB CE2 
3658 C  CZ  . TYR   B 205 ? 0.623 0.447 0.528 0.141  0.082  0.114  204 TYR   BBB CZ  
3659 O  OH  . TYR   B 205 ? 0.623 0.264 0.521 -0.105 0.050  0.014  204 TYR   BBB OH  
3660 N  N   . GLU   B 206 ? 0.259 0.088 0.480 0.021  -0.000 0.042  205 GLU   BBB N   
3661 C  CA  . GLU   B 206 ? 0.317 0.175 0.470 -0.009 -0.001 0.062  205 GLU   BBB CA  
3662 C  C   . GLU   B 206 ? 0.310 0.144 0.501 0.040  -0.002 0.023  205 GLU   BBB C   
3663 O  O   . GLU   B 206 ? 0.338 0.139 0.528 -0.017 -0.036 0.027  205 GLU   BBB O   
3664 C  CB  . GLU   B 206 ? 0.285 0.224 0.467 0.063  -0.061 0.025  205 GLU   BBB CB  
3665 C  CG  . GLU   B 206 ? 0.296 0.128 0.533 0.088  -0.017 0.017  205 GLU   BBB CG  
3666 C  CD  . GLU   B 206 ? 0.302 0.123 0.567 0.008  0.004  0.085  205 GLU   BBB CD  
3667 O  OE1 . GLU   B 206 ? 0.367 0.008 0.570 0.028  0.076  0.006  205 GLU   BBB OE1 
3668 O  OE2 . GLU   B 206 ? 0.340 0.203 0.606 0.007  -0.014 0.081  205 GLU   BBB OE2 
3669 N  N   . SER   B 207 ? 0.309 0.120 0.476 -0.002 0.046  0.059  206 SER   BBB N   
3670 C  CA  . SER   B 207 ? 0.245 0.182 0.404 -0.041 -0.001 0.054  206 SER   BBB CA  
3671 C  C   . SER   B 207 ? 0.285 0.171 0.411 -0.028 0.047  0.087  206 SER   BBB C   
3672 O  O   . SER   B 207 ? 0.312 0.188 0.516 -0.054 -0.004 0.069  206 SER   BBB O   
3673 C  CB  . SER   B 207 ? 0.343 0.139 0.450 0.020  0.010  0.100  206 SER   BBB CB  
3674 O  OG  . SER   B 207 ? 0.341 0.133 0.509 0.013  0.013  0.080  206 SER   BBB OG  
3675 N  N   . VAL   B 208 ? 0.240 0.094 0.463 0.014  0.013  0.133  207 VAL   BBB N   
3676 C  CA  . VAL   B 208 ? 0.275 0.026 0.461 0.014  0.006  0.094  207 VAL   BBB CA  
3677 C  C   . VAL   B 208 ? 0.347 0.028 0.455 0.017  -0.077 0.048  207 VAL   BBB C   
3678 O  O   . VAL   B 208 ? 0.400 0.073 0.393 -0.013 -0.020 0.074  207 VAL   BBB O   
3679 C  CB  . VAL   B 208 ? 0.279 0.056 0.418 -0.026 0.031  0.048  207 VAL   BBB CB  
3680 C  CG1 . VAL   B 208 ? 0.279 0.010 0.451 -0.007 -0.001 0.039  207 VAL   BBB CG1 
3681 C  CG2 . VAL   B 208 ? 0.354 0.038 0.434 -0.061 0.021  0.019  207 VAL   BBB CG2 
3682 N  N   . THR   B 209 ? 0.281 0.066 0.422 -0.026 -0.023 0.013  208 THR   BBB N   
3683 C  CA  . THR   B 209 ? 0.285 0.024 0.437 -0.050 -0.028 0.057  208 THR   BBB CA  
3684 C  C   . THR   B 209 ? 0.248 0.053 0.399 -0.073 -0.043 0.081  208 THR   BBB C   
3685 O  O   . THR   B 209 ? 0.308 0.041 0.458 -0.035 -0.016 0.073  208 THR   BBB O   
3686 C  CB  . THR   B 209 ? 0.286 0.019 0.484 -0.043 -0.051 0.060  208 THR   BBB CB  
3687 O  OG1 . THR   B 209 ? 0.287 0.072 0.476 -0.046 -0.032 0.052  208 THR   BBB OG1 
3688 C  CG2 . THR   B 209 ? 0.414 0.025 0.477 -0.050 -0.031 0.080  208 THR   BBB CG2 
3689 N  N   . TRP   B 210 ? 0.288 0.027 0.462 -0.033 -0.020 0.091  209 TRP   BBB N   
3690 C  CA  . TRP   B 210 ? 0.293 0.019 0.381 -0.016 0.015  0.066  209 TRP   BBB CA  
3691 C  C   . TRP   B 210 ? 0.274 0.060 0.378 -0.009 -0.037 0.048  209 TRP   BBB C   
3692 O  O   . TRP   B 210 ? 0.329 0.037 0.408 -0.023 -0.037 0.050  209 TRP   BBB O   
3693 C  CB  . TRP   B 210 ? 0.281 0.018 0.396 0.005  -0.010 0.067  209 TRP   BBB CB  
3694 C  CG  . TRP   B 210 ? 0.236 0.022 0.384 -0.023 -0.009 0.044  209 TRP   BBB CG  
3695 C  CD1 . TRP   B 210 ? 0.279 0.054 0.400 0.006  -0.029 0.004  209 TRP   BBB CD1 
3696 C  CD2 . TRP   B 210 ? 0.249 0.022 0.364 -0.034 -0.025 0.036  209 TRP   BBB CD2 
3697 N  NE1 . TRP   B 210 ? 0.295 0.035 0.418 -0.004 -0.020 -0.001 209 TRP   BBB NE1 
3698 C  CE2 . TRP   B 210 ? 0.244 0.088 0.380 -0.019 0.013  0.051  209 TRP   BBB CE2 
3699 C  CE3 . TRP   B 210 ? 0.250 0.035 0.357 -0.027 -0.007 0.048  209 TRP   BBB CE3 
3700 C  CZ2 . TRP   B 210 ? 0.282 0.039 0.419 -0.051 -0.015 0.032  209 TRP   BBB CZ2 
3701 C  CZ3 . TRP   B 210 ? 0.303 0.088 0.365 -0.039 -0.038 0.013  209 TRP   BBB CZ3 
3702 C  CH2 . TRP   B 210 ? 0.311 0.030 0.381 -0.036 -0.005 0.035  209 TRP   BBB CH2 
3703 N  N   . ILE   B 211 ? 0.279 0.052 0.390 -0.006 -0.020 0.114  210 ILE   BBB N   
3704 C  CA  . ILE   B 211 ? 0.322 0.042 0.407 -0.085 0.011  0.069  210 ILE   BBB CA  
3705 C  C   . ILE   B 211 ? 0.312 0.038 0.394 -0.037 0.012  0.058  210 ILE   BBB C   
3706 O  O   . ILE   B 211 ? 0.361 0.022 0.453 -0.054 -0.033 0.064  210 ILE   BBB O   
3707 C  CB  . ILE   B 211 ? 0.332 0.057 0.389 -0.095 0.001  0.093  210 ILE   BBB CB  
3708 C  CG1 . ILE   B 211 ? 0.348 0.049 0.440 -0.037 0.001  0.024  210 ILE   BBB CG1 
3709 C  CG2 . ILE   B 211 ? 0.356 0.027 0.455 -0.073 -0.018 0.051  210 ILE   BBB CG2 
3710 C  CD1 . ILE   B 211 ? 0.420 0.017 0.529 -0.047 -0.038 0.052  210 ILE   BBB CD1 
3711 N  N   . ILE   B 212 ? 0.310 0.019 0.404 0.031  -0.006 0.063  211 ILE   BBB N   
3712 C  CA  . ILE   B 212 ? 0.292 0.033 0.396 0.033  0.018  0.096  211 ILE   BBB CA  
3713 C  C   . ILE   B 212 ? 0.220 0.021 0.382 0.004  -0.041 0.072  211 ILE   BBB C   
3714 O  O   . ILE   B 212 ? 0.295 0.011 0.417 0.017  -0.058 0.037  211 ILE   BBB O   
3715 C  CB  . ILE   B 212 ? 0.356 0.027 0.379 -0.026 0.008  0.082  211 ILE   BBB CB  
3716 C  CG1 . ILE   B 212 ? 0.333 0.026 0.390 -0.061 0.034  0.050  211 ILE   BBB CG1 
3717 C  CG2 . ILE   B 212 ? 0.352 0.013 0.397 0.007  -0.007 0.051  211 ILE   BBB CG2 
3718 C  CD1 . ILE   B 212 ? 0.336 0.010 0.383 -0.016 0.035  0.032  211 ILE   BBB CD1 
3719 N  N   . CYS   B 213 ? 0.356 0.011 0.440 -0.014 -0.052 0.043  212 CYS   BBB N   
3720 C  CA  . CYS   B 213 ? 0.333 0.064 0.364 -0.021 -0.041 0.045  212 CYS   BBB CA  
3721 C  C   . CYS   B 213 ? 0.301 0.020 0.356 0.030  -0.034 0.022  212 CYS   BBB C   
3722 O  O   . CYS   B 213 ? 0.313 0.008 0.364 -0.005 -0.022 0.024  212 CYS   BBB O   
3723 C  CB  . CYS   B 213 ? 0.337 0.013 0.419 -0.041 -0.015 0.026  212 CYS   BBB CB  
3724 S  SG  . CYS   B 213 ? 0.387 0.009 0.502 -0.013 -0.025 0.034  212 CYS   BBB SG  
3725 N  N   . LYS   B 214 ? 0.310 0.024 0.368 0.045  -0.018 0.017  213 LYS   BBB N   
3726 C  CA  . LYS   B 214 ? 0.332 0.015 0.352 0.048  0.015  -0.019 213 LYS   BBB CA  
3727 C  C   . LYS   B 214 ? 0.304 0.007 0.389 -0.006 -0.010 0.009  213 LYS   BBB C   
3728 O  O   . LYS   B 214 ? 0.348 0.014 0.470 -0.038 0.009  0.034  213 LYS   BBB O   
3729 C  CB  . LYS   B 214 ? 0.374 0.171 0.367 0.061  -0.023 -0.016 213 LYS   BBB CB  
3730 C  CG  . LYS   B 214 ? 0.404 0.141 0.492 -0.000 -0.026 0.051  213 LYS   BBB CG  
3731 C  CD  . LYS   B 214 ? 0.431 0.382 0.518 0.077  -0.047 -0.035 213 LYS   BBB CD  
3732 C  CE  . LYS   B 214 ? 0.605 0.397 0.560 0.010  0.048  -0.053 213 LYS   BBB CE  
3733 N  NZ  . LYS   B 214 ? 0.632 0.645 0.632 -0.108 0.153  -0.217 213 LYS   BBB NZ  
3734 N  N   . GLU   B 215 ? 0.345 0.009 0.377 0.018  -0.001 0.022  214 GLU   BBB N   
3735 C  CA  . GLU   B 215 ? 0.323 0.035 0.382 -0.006 0.004  -0.020 214 GLU   BBB CA  
3736 C  C   . GLU   B 215 ? 0.296 0.013 0.384 0.042  -0.004 -0.010 214 GLU   BBB C   
3737 O  O   . GLU   B 215 ? 0.378 0.007 0.375 0.010  -0.006 0.015  214 GLU   BBB O   
3738 C  CB  . GLU   B 215 ? 0.386 0.071 0.408 -0.015 0.013  -0.088 214 GLU   BBB CB  
3739 C  CG  . GLU   B 215 ? 0.477 0.066 0.480 0.031  -0.012 -0.154 214 GLU   BBB CG  
3740 C  CD  . GLU   B 215 ? 0.509 0.345 0.594 -0.056 -0.007 -0.055 214 GLU   BBB CD  
3741 O  OE1 . GLU   B 215 ? 0.494 0.464 0.654 -0.052 -0.066 -0.085 214 GLU   BBB OE1 
3742 O  OE2 . GLU   B 215 ? 0.683 0.494 0.581 0.094  0.002  0.018  214 GLU   BBB OE2 
3743 N  N   . SER   B 216 ? 0.317 0.013 0.460 0.015  -0.001 0.054  215 SER   BBB N   
3744 C  CA  . SER   B 216 ? 0.351 0.010 0.437 -0.001 -0.018 0.042  215 SER   BBB CA  
3745 C  C   . SER   B 216 ? 0.336 0.020 0.369 0.038  -0.017 0.055  215 SER   BBB C   
3746 O  O   . SER   B 216 ? 0.388 0.032 0.412 -0.016 -0.059 0.005  215 SER   BBB O   
3747 C  CB  . SER   B 216 ? 0.293 0.023 0.435 -0.068 0.002  -0.011 215 SER   BBB CB  
3748 O  OG  . SER   B 216 ? 0.361 0.092 0.451 -0.082 0.038  0.003  215 SER   BBB OG  
3749 N  N   . ILE   B 217 ? 0.345 0.012 0.394 0.032  -0.043 0.030  216 ILE   BBB N   
3750 C  CA  . ILE   B 217 ? 0.320 0.015 0.350 0.050  -0.045 0.006  216 ILE   BBB CA  
3751 C  C   . ILE   B 217 ? 0.297 0.010 0.418 0.032  -0.022 -0.006 216 ILE   BBB C   
3752 O  O   . ILE   B 217 ? 0.336 0.008 0.436 0.019  -0.021 0.007  216 ILE   BBB O   
3753 C  CB  . ILE   B 217 ? 0.326 0.098 0.352 -0.005 -0.017 -0.007 216 ILE   BBB CB  
3754 C  CG1 . ILE   B 217 ? 0.340 0.024 0.385 0.007  -0.006 -0.017 216 ILE   BBB CG1 
3755 C  CG2 . ILE   B 217 ? 0.372 0.007 0.378 0.016  -0.035 -0.010 216 ILE   BBB CG2 
3756 C  CD1 . ILE   B 217 ? 0.319 0.038 0.353 0.049  -0.006 -0.019 216 ILE   BBB CD1 
3757 N  N   . SER   B 218 ? 0.346 0.015 0.440 0.053  -0.013 0.015  217 SER   BBB N   
3758 C  CA  A SER   B 218 ? 0.328 0.019 0.432 0.064  0.004  -0.007 217 SER   BBB CA  
3759 C  CA  B SER   B 218 ? 0.333 0.011 0.430 0.041  0.012  0.003  217 SER   BBB CA  
3760 C  C   . SER   B 218 ? 0.239 0.023 0.422 0.057  0.028  -0.029 217 SER   BBB C   
3761 O  O   . SER   B 218 ? 0.289 0.057 0.401 0.001  0.018  -0.024 217 SER   BBB O   
3762 C  CB  A SER   B 218 ? 0.311 0.063 0.430 0.087  0.003  -0.011 217 SER   BBB CB  
3763 C  CB  B SER   B 218 ? 0.312 0.099 0.415 0.070  0.016  -0.012 217 SER   BBB CB  
3764 O  OG  A SER   B 218 ? 0.401 0.040 0.437 0.051  0.027  0.003  217 SER   BBB OG  
3765 O  OG  B SER   B 218 ? 0.345 0.148 0.433 0.031  0.042  -0.027 217 SER   BBB OG  
3766 N  N   . VAL   B 219 ? 0.268 0.047 0.393 0.023  -0.011 0.032  218 VAL   BBB N   
3767 C  CA  . VAL   B 219 ? 0.293 0.041 0.378 0.029  -0.001 0.013  218 VAL   BBB CA  
3768 C  C   . VAL   B 219 ? 0.253 0.159 0.355 0.044  0.011  0.040  218 VAL   BBB C   
3769 O  O   . VAL   B 219 ? 0.306 0.054 0.424 -0.000 0.018  0.014  218 VAL   BBB O   
3770 C  CB  . VAL   B 219 ? 0.269 0.048 0.394 -0.022 0.001  -0.038 218 VAL   BBB CB  
3771 C  CG1 . VAL   B 219 ? 0.315 0.063 0.456 0.008  -0.031 0.004  218 VAL   BBB CG1 
3772 C  CG2 . VAL   B 219 ? 0.298 0.032 0.398 -0.005 -0.008 -0.009 218 VAL   BBB CG2 
3773 N  N   . SER   B 220 ? 0.273 0.064 0.399 0.070  -0.026 -0.047 219 SER   BBB N   
3774 C  CA  . SER   B 220 ? 0.269 0.169 0.372 0.050  -0.019 -0.043 219 SER   BBB CA  
3775 C  C   . SER   B 220 ? 0.225 0.104 0.381 0.040  0.006  -0.026 219 SER   BBB C   
3776 O  O   . SER   B 220 ? 0.278 0.043 0.396 0.003  -0.000 -0.016 219 SER   BBB O   
3777 C  CB  . SER   B 220 ? 0.283 0.154 0.410 0.036  -0.022 -0.027 219 SER   BBB CB  
3778 O  OG  . SER   B 220 ? 0.331 0.141 0.423 0.058  -0.003 -0.016 219 SER   BBB OG  
3779 N  N   . SER   B 221 ? 0.234 0.220 0.373 0.001  0.002  -0.016 220 SER   BBB N   
3780 C  CA  . SER   B 221 ? 0.302 0.135 0.396 -0.013 -0.009 -0.005 220 SER   BBB CA  
3781 C  C   . SER   B 221 ? 0.287 0.196 0.371 0.034  -0.011 -0.059 220 SER   BBB C   
3782 O  O   . SER   B 221 ? 0.330 0.061 0.379 -0.003 0.024  -0.002 220 SER   BBB O   
3783 C  CB  . SER   B 221 ? 0.307 0.347 0.413 -0.094 0.003  -0.077 220 SER   BBB CB  
3784 O  OG  . SER   B 221 ? 0.403 0.224 0.533 -0.012 0.002  -0.052 220 SER   BBB OG  
3785 N  N   . GLU   B 222 ? 0.271 0.147 0.422 -0.006 0.003  0.007  221 GLU   BBB N   
3786 C  CA  . GLU   B 222 ? 0.258 0.124 0.405 0.029  -0.004 -0.035 221 GLU   BBB CA  
3787 C  C   . GLU   B 222 ? 0.250 0.105 0.364 0.056  -0.030 0.009  221 GLU   BBB C   
3788 O  O   . GLU   B 222 ? 0.299 0.054 0.396 0.007  0.008  -0.004 221 GLU   BBB O   
3789 C  CB  . GLU   B 222 ? 0.279 0.181 0.404 0.060  0.018  -0.016 221 GLU   BBB CB  
3790 C  CG  . GLU   B 222 ? 0.290 0.285 0.392 0.056  0.036  -0.049 221 GLU   BBB CG  
3791 C  CD  . GLU   B 222 ? 0.267 0.268 0.397 0.030  -0.035 0.005  221 GLU   BBB CD  
3792 O  OE1 . GLU   B 222 ? 0.348 0.323 0.415 0.052  -0.034 -0.054 221 GLU   BBB OE1 
3793 O  OE2 . GLU   B 222 ? 0.329 0.289 0.453 -0.018 -0.000 -0.022 221 GLU   BBB OE2 
3794 N  N   . GLN   B 223 ? 0.274 0.076 0.391 0.035  -0.025 -0.007 222 GLN   BBB N   
3795 C  CA  . GLN   B 223 ? 0.276 0.078 0.387 0.049  -0.003 -0.023 222 GLN   BBB CA  
3796 C  C   . GLN   B 223 ? 0.275 0.058 0.382 0.017  0.046  -0.023 222 GLN   BBB C   
3797 O  O   . GLN   B 223 ? 0.288 0.011 0.403 0.026  0.035  -0.025 222 GLN   BBB O   
3798 C  CB  . GLN   B 223 ? 0.307 0.014 0.389 0.025  0.003  -0.045 222 GLN   BBB CB  
3799 C  CG  . GLN   B 223 ? 0.335 0.015 0.429 0.053  -0.007 0.007  222 GLN   BBB CG  
3800 C  CD  . GLN   B 223 ? 0.393 0.007 0.389 -0.008 0.033  0.016  222 GLN   BBB CD  
3801 O  OE1 . GLN   B 223 ? 0.390 0.009 0.424 0.027  -0.022 -0.017 222 GLN   BBB OE1 
3802 N  NE2 . GLN   B 223 ? 0.391 0.009 0.444 0.031  -0.011 -0.002 222 GLN   BBB NE2 
3803 N  N   . LEU   B 224 ? 0.279 0.111 0.350 -0.002 0.018  -0.001 223 LEU   BBB N   
3804 C  CA  . LEU   B 224 ? 0.291 0.134 0.370 0.036  0.017  0.012  223 LEU   BBB CA  
3805 C  C   . LEU   B 224 ? 0.255 0.078 0.392 0.038  -0.002 0.054  223 LEU   BBB C   
3806 O  O   . LEU   B 224 ? 0.277 0.086 0.449 0.021  0.003  -0.053 223 LEU   BBB O   
3807 C  CB  . LEU   B 224 ? 0.323 0.037 0.380 0.010  -0.012 -0.013 223 LEU   BBB CB  
3808 C  CG  . LEU   B 224 ? 0.342 0.111 0.400 0.026  -0.023 -0.007 223 LEU   BBB CG  
3809 C  CD1 . LEU   B 224 ? 0.427 0.162 0.414 0.033  -0.013 0.021  223 LEU   BBB CD1 
3810 C  CD2 . LEU   B 224 ? 0.337 0.227 0.464 0.080  -0.018 -0.063 223 LEU   BBB CD2 
3811 N  N   . ALA   B 225 ? 0.262 0.019 0.424 0.055  -0.016 -0.022 224 ALA   BBB N   
3812 C  CA  . ALA   B 225 ? 0.279 0.038 0.442 0.026  -0.028 -0.026 224 ALA   BBB CA  
3813 C  C   . ALA   B 225 ? 0.290 0.081 0.412 0.021  0.010  -0.050 224 ALA   BBB C   
3814 O  O   . ALA   B 225 ? 0.327 0.125 0.387 0.020  0.011  0.008  224 ALA   BBB O   
3815 C  CB  . ALA   B 225 ? 0.292 0.077 0.488 0.024  0.022  -0.075 224 ALA   BBB CB  
3816 N  N   . GLN   B 226 ? 0.297 0.067 0.434 0.061  0.007  -0.063 225 GLN   BBB N   
3817 C  CA  . GLN   B 226 ? 0.324 0.126 0.440 0.032  0.007  -0.048 225 GLN   BBB CA  
3818 C  C   . GLN   B 226 ? 0.283 0.136 0.371 0.001  -0.034 -0.019 225 GLN   BBB C   
3819 O  O   . GLN   B 226 ? 0.331 0.076 0.380 0.005  -0.019 -0.026 225 GLN   BBB O   
3820 C  CB  . GLN   B 226 ? 0.344 0.103 0.462 0.009  -0.026 -0.027 225 GLN   BBB CB  
3821 C  CG  . GLN   B 226 ? 0.323 0.097 0.514 0.007  -0.058 -0.051 225 GLN   BBB CG  
3822 C  CD  . GLN   B 226 ? 0.335 0.092 0.485 0.001  0.005  -0.044 225 GLN   BBB CD  
3823 O  OE1 . GLN   B 226 ? 0.370 0.159 0.527 0.054  -0.035 -0.094 225 GLN   BBB OE1 
3824 N  NE2 . GLN   B 226 ? 0.362 0.200 0.429 0.002  -0.007 -0.036 225 GLN   BBB NE2 
3825 N  N   . PHE   B 227 ? 0.281 0.052 0.381 0.015  -0.027 -0.016 226 PHE   BBB N   
3826 C  CA  . PHE   B 227 ? 0.259 0.123 0.421 -0.011 -0.016 -0.024 226 PHE   BBB CA  
3827 C  C   . PHE   B 227 ? 0.241 0.064 0.408 0.063  0.000  0.012  226 PHE   BBB C   
3828 O  O   . PHE   B 227 ? 0.291 0.048 0.439 -0.003 0.023  -0.018 226 PHE   BBB O   
3829 C  CB  . PHE   B 227 ? 0.300 0.009 0.439 0.015  -0.005 -0.017 226 PHE   BBB CB  
3830 C  CG  . PHE   B 227 ? 0.298 0.030 0.439 0.006  -0.009 -0.025 226 PHE   BBB CG  
3831 C  CD1 . PHE   B 227 ? 0.397 0.073 0.455 -0.092 0.026  0.001  226 PHE   BBB CD1 
3832 C  CD2 . PHE   B 227 ? 0.371 0.166 0.442 0.031  -0.015 -0.032 226 PHE   BBB CD2 
3833 C  CE1 . PHE   B 227 ? 0.355 0.286 0.428 -0.036 -0.012 -0.063 226 PHE   BBB CE1 
3834 C  CE2 . PHE   B 227 ? 0.362 0.198 0.448 0.065  -0.016 -0.070 226 PHE   BBB CE2 
3835 C  CZ  . PHE   B 227 ? 0.322 0.276 0.435 -0.077 -0.019 -0.040 226 PHE   BBB CZ  
3836 N  N   . ARG   B 228 ? 0.273 0.088 0.406 0.015  0.009  -0.009 227 ARG   BBB N   
3837 C  CA  . ARG   B 228 ? 0.278 0.114 0.417 0.021  0.020  -0.032 227 ARG   BBB CA  
3838 C  C   . ARG   B 228 ? 0.319 0.063 0.401 0.056  0.024  -0.028 227 ARG   BBB C   
3839 O  O   . ARG   B 228 ? 0.424 0.103 0.471 -0.032 0.011  -0.071 227 ARG   BBB O   
3840 C  CB  . ARG   B 228 ? 0.290 0.067 0.462 -0.006 0.014  -0.030 227 ARG   BBB CB  
3841 C  CG  . ARG   B 228 ? 0.308 0.075 0.499 -0.015 0.017  0.008  227 ARG   BBB CG  
3842 C  CD  . ARG   B 228 ? 0.361 0.061 0.500 -0.048 0.018  -0.048 227 ARG   BBB CD  
3843 N  NE  . ARG   B 228 ? 0.405 0.132 0.520 -0.045 0.020  0.008  227 ARG   BBB NE  
3844 C  CZ  . ARG   B 228 ? 0.382 0.163 0.538 -0.012 0.014  -0.022 227 ARG   BBB CZ  
3845 N  NH1 . ARG   B 228 ? 0.573 0.144 0.561 -0.039 -0.042 -0.021 227 ARG   BBB NH1 
3846 N  NH2 . ARG   B 228 ? 0.394 0.133 0.523 0.021  -0.001 0.025  227 ARG   BBB NH2 
3847 N  N   . SER   B 229 ? 0.270 0.032 0.402 0.023  0.031  -0.049 228 SER   BBB N   
3848 C  CA  . SER   B 229 ? 0.306 0.117 0.393 0.027  0.020  -0.052 228 SER   BBB CA  
3849 C  C   . SER   B 229 ? 0.259 0.095 0.397 0.023  -0.006 -0.053 228 SER   BBB C   
3850 O  O   . SER   B 229 ? 0.308 0.212 0.389 0.000  -0.017 -0.061 228 SER   BBB O   
3851 C  CB  . SER   B 229 ? 0.384 0.231 0.440 0.109  0.025  -0.093 228 SER   BBB CB  
3852 O  OG  . SER   B 229 ? 0.582 0.277 0.584 0.023  -0.070 0.008  228 SER   BBB OG  
3853 N  N   . LEU   B 230 ? 0.269 0.051 0.419 0.001  0.006  -0.073 229 LEU   BBB N   
3854 C  CA  . LEU   B 230 ? 0.259 0.061 0.439 -0.007 0.004  -0.079 229 LEU   BBB CA  
3855 C  C   . LEU   B 230 ? 0.266 0.063 0.379 0.024  0.047  -0.052 229 LEU   BBB C   
3856 O  O   . LEU   B 230 ? 0.365 0.136 0.436 -0.064 0.006  0.028  229 LEU   BBB O   
3857 C  CB  . LEU   B 230 ? 0.311 0.113 0.367 -0.057 -0.018 -0.040 229 LEU   BBB CB  
3858 C  CG  . LEU   B 230 ? 0.403 0.138 0.438 -0.039 -0.042 -0.082 229 LEU   BBB CG  
3859 C  CD1 . LEU   B 230 ? 0.356 0.194 0.536 -0.051 -0.051 -0.082 229 LEU   BBB CD1 
3860 C  CD2 . LEU   B 230 ? 0.408 0.197 0.473 -0.018 -0.006 -0.024 229 LEU   BBB CD2 
3861 N  N   . LEU   B 231 ? 0.276 0.093 0.355 0.002  0.000  -0.030 230 LEU   BBB N   
3862 C  CA  . LEU   B 231 ? 0.273 0.177 0.362 -0.036 0.003  -0.074 230 LEU   BBB CA  
3863 C  C   . LEU   B 231 ? 0.261 0.156 0.461 -0.056 0.007  -0.010 230 LEU   BBB C   
3864 O  O   . LEU   B 231 ? 0.287 0.031 0.444 -0.028 -0.019 -0.050 230 LEU   BBB O   
3865 C  CB  . LEU   B 231 ? 0.317 0.074 0.394 -0.030 -0.002 -0.064 230 LEU   BBB CB  
3866 C  CG  . LEU   B 231 ? 0.312 0.100 0.421 -0.014 -0.004 -0.007 230 LEU   BBB CG  
3867 C  CD1 . LEU   B 231 ? 0.359 0.250 0.457 -0.038 -0.012 0.059  230 LEU   BBB CD1 
3868 C  CD2 . LEU   B 231 ? 0.350 0.170 0.414 -0.026 0.019  0.028  230 LEU   BBB CD2 
3869 N  N   . SER   B 232 ? 0.323 0.159 0.406 -0.003 -0.009 -0.029 231 SER   BBB N   
3870 C  CA  . SER   B 232 ? 0.340 0.031 0.459 0.019  -0.013 -0.031 231 SER   BBB CA  
3871 C  C   . SER   B 232 ? 0.286 0.008 0.451 0.021  -0.037 -0.006 231 SER   BBB C   
3872 O  O   . SER   B 232 ? 0.314 0.101 0.474 0.020  0.028  -0.097 231 SER   BBB O   
3873 C  CB  . SER   B 232 ? 0.332 0.033 0.475 0.005  -0.026 -0.023 231 SER   BBB CB  
3874 O  OG  . SER   B 232 ? 0.383 0.063 0.569 -0.030 -0.036 -0.044 231 SER   BBB OG  
3875 N  N   . ASN   B 233 ? 0.277 0.050 0.434 0.060  -0.027 -0.040 232 ASN   BBB N   
3876 C  CA  . ASN   B 233 ? 0.342 0.106 0.438 0.078  -0.016 -0.023 232 ASN   BBB CA  
3877 C  C   . ASN   B 233 ? 0.329 0.160 0.352 0.013  -0.003 -0.048 232 ASN   BBB C   
3878 O  O   . ASN   B 233 ? 0.319 0.136 0.398 0.033  0.022  -0.047 232 ASN   BBB O   
3879 C  CB  . ASN   B 233 ? 0.363 0.054 0.462 0.062  -0.035 -0.066 232 ASN   BBB CB  
3880 C  CG  . ASN   B 233 ? 0.262 0.207 0.362 0.063  -0.026 -0.042 232 ASN   BBB CG  
3881 O  OD1 . ASN   B 233 ? 0.304 0.164 0.449 -0.021 0.031  -0.066 232 ASN   BBB OD1 
3882 N  ND2 . ASN   B 233 ? 0.321 0.092 0.374 0.034  -0.043 -0.048 232 ASN   BBB ND2 
3883 N  N   . VAL   B 234 ? 0.346 0.168 0.391 0.026  0.034  -0.053 233 VAL   BBB N   
3884 C  CA  . VAL   B 234 ? 0.308 0.108 0.402 0.016  -0.011 -0.091 233 VAL   BBB CA  
3885 C  C   . VAL   B 234 ? 0.287 0.263 0.421 0.009  -0.014 -0.045 233 VAL   BBB C   
3886 O  O   . VAL   B 234 ? 0.288 0.273 0.434 0.022  -0.009 -0.105 233 VAL   BBB O   
3887 C  CB  . VAL   B 234 ? 0.353 0.318 0.445 -0.019 0.022  -0.068 233 VAL   BBB CB  
3888 C  CG1 . VAL   B 234 ? 0.391 0.270 0.445 -0.066 0.006  -0.041 233 VAL   BBB CG1 
3889 C  CG2 . VAL   B 234 ? 0.367 0.319 0.487 0.014  0.050  -0.108 233 VAL   BBB CG2 
3890 N  N   . GLU   B 235 ? 0.305 0.258 0.442 0.025  -0.004 -0.075 234 GLU   BBB N   
3891 C  CA  . GLU   B 235 ? 0.339 0.249 0.390 0.033  -0.015 -0.052 234 GLU   BBB CA  
3892 C  C   . GLU   B 235 ? 0.299 0.270 0.386 0.006  -0.023 -0.046 234 GLU   BBB C   
3893 O  O   . GLU   B 235 ? 0.377 0.353 0.415 -0.025 0.027  -0.067 234 GLU   BBB O   
3894 C  CB  . GLU   B 235 ? 0.341 0.268 0.440 0.008  -0.010 -0.028 234 GLU   BBB CB  
3895 C  CG  . GLU   B 235 ? 0.337 0.298 0.500 0.022  -0.033 0.005  234 GLU   BBB CG  
3896 C  CD  . GLU   B 235 ? 0.523 0.304 0.487 0.066  -0.022 0.088  234 GLU   BBB CD  
3897 O  OE1 . GLU   B 235 ? 0.497 0.317 0.588 -0.015 -0.049 0.067  234 GLU   BBB OE1 
3898 O  OE2 . GLU   B 235 ? 0.787 0.390 0.428 0.088  -0.014 0.036  234 GLU   BBB OE2 
3899 N  N   . GLY   B 236 ? 0.283 0.216 0.453 0.040  0.016  -0.067 235 GLY   BBB N   
3900 C  CA  . GLY   B 236 ? 0.398 0.317 0.488 -0.052 -0.055 -0.039 235 GLY   BBB CA  
3901 C  C   . GLY   B 236 ? 0.406 0.302 0.370 -0.003 -0.042 0.004  235 GLY   BBB C   
3902 O  O   . GLY   B 236 ? 0.494 0.425 0.543 -0.070 -0.080 -0.047 235 GLY   BBB O   
3903 N  N   . ASP   B 237 ? 0.322 0.217 0.414 -0.034 -0.016 0.014  236 ASP   BBB N   
3904 C  CA  . ASP   B 237 ? 0.418 0.199 0.469 -0.099 0.024  -0.087 236 ASP   BBB CA  
3905 C  C   . ASP   B 237 ? 0.402 0.099 0.466 -0.105 0.025  -0.055 236 ASP   BBB C   
3906 O  O   . ASP   B 237 ? 0.404 0.284 0.516 -0.031 0.047  -0.123 236 ASP   BBB O   
3907 C  CB  . ASP   B 237 ? 0.427 0.211 0.453 -0.084 0.036  -0.105 236 ASP   BBB CB  
3908 C  CG  . ASP   B 237 ? 0.448 0.274 0.415 -0.023 0.010  -0.127 236 ASP   BBB CG  
3909 O  OD1 . ASP   B 237 ? 0.484 0.478 0.407 0.062  0.025  -0.112 236 ASP   BBB OD1 
3910 O  OD2 . ASP   B 237 ? 0.463 0.196 0.612 0.074  0.015  -0.092 236 ASP   BBB OD2 
3911 N  N   . ASN   B 238 ? 0.426 0.125 0.459 -0.142 0.051  -0.060 237 ASN   BBB N   
3912 C  CA  . ASN   B 238 ? 0.423 0.187 0.458 -0.184 0.006  -0.022 237 ASN   BBB CA  
3913 C  C   . ASN   B 238 ? 0.344 0.189 0.454 -0.111 0.014  -0.077 237 ASN   BBB C   
3914 O  O   . ASN   B 238 ? 0.353 0.226 0.495 -0.039 0.005  -0.087 237 ASN   BBB O   
3915 C  CB  . ASN   B 238 ? 0.458 0.131 0.497 -0.121 -0.006 -0.025 237 ASN   BBB CB  
3916 C  CG  . ASN   B 238 ? 0.321 0.261 0.574 -0.068 -0.044 0.044  237 ASN   BBB CG  
3917 O  OD1 . ASN   B 238 ? 0.354 0.328 0.688 -0.007 -0.052 0.155  237 ASN   BBB OD1 
3918 N  ND2 . ASN   B 238 ? 0.510 0.367 0.695 0.011  -0.047 0.158  237 ASN   BBB ND2 
3919 N  N   . ALA   B 239 ? 0.345 0.394 0.472 -0.090 0.046  -0.103 238 ALA   BBB N   
3920 C  CA  . ALA   B 239 ? 0.390 0.399 0.479 0.011  0.038  -0.146 238 ALA   BBB CA  
3921 C  C   . ALA   B 239 ? 0.293 0.319 0.471 -0.131 0.010  -0.144 238 ALA   BBB C   
3922 O  O   . ALA   B 239 ? 0.433 0.536 0.579 -0.309 -0.059 -0.027 238 ALA   BBB O   
3923 C  CB  . ALA   B 239 ? 0.303 0.476 0.457 0.011  0.027  -0.174 238 ALA   BBB CB  
3924 N  N   . VAL   B 240 ? 0.327 0.333 0.453 -0.070 -0.021 -0.082 239 VAL   BBB N   
3925 C  CA  . VAL   B 240 ? 0.334 0.144 0.467 -0.101 -0.013 -0.075 239 VAL   BBB CA  
3926 C  C   . VAL   B 240 ? 0.296 0.143 0.441 -0.000 0.007  -0.061 239 VAL   BBB C   
3927 O  O   . VAL   B 240 ? 0.359 0.134 0.475 -0.068 0.015  0.007  239 VAL   BBB O   
3928 C  CB  . VAL   B 240 ? 0.448 0.259 0.501 -0.022 0.038  -0.092 239 VAL   BBB CB  
3929 C  CG1 . VAL   B 240 ? 0.825 0.066 0.593 -0.087 0.030  -0.175 239 VAL   BBB CG1 
3930 C  CG2 . VAL   B 240 ? 0.483 0.218 0.491 0.030  -0.018 -0.063 239 VAL   BBB CG2 
3931 N  N   . PRO   B 241 ? 0.336 0.143 0.423 -0.032 0.022  -0.023 240 PRO   BBB N   
3932 C  CA  . PRO   B 241 ? 0.320 0.213 0.422 -0.014 -0.024 -0.043 240 PRO   BBB CA  
3933 C  C   . PRO   B 241 ? 0.322 0.154 0.375 -0.049 -0.067 -0.136 240 PRO   BBB C   
3934 O  O   . PRO   B 241 ? 0.430 0.110 0.480 -0.041 -0.016 -0.080 240 PRO   BBB O   
3935 C  CB  . PRO   B 241 ? 0.351 0.297 0.478 -0.018 0.015  -0.061 240 PRO   BBB CB  
3936 C  CG  . PRO   B 241 ? 0.385 0.420 0.477 -0.018 -0.003 -0.008 240 PRO   BBB CG  
3937 C  CD  . PRO   B 241 ? 0.339 0.225 0.495 -0.041 -0.001 -0.003 240 PRO   BBB CD  
3938 N  N   . MET   B 242 ? 0.395 0.020 0.464 -0.032 0.012  -0.073 241 MET   BBB N   
3939 C  CA  . MET   B 242 ? 0.352 0.022 0.478 0.006  0.021  -0.086 241 MET   BBB CA  
3940 C  C   . MET   B 242 ? 0.337 0.108 0.442 -0.003 -0.010 -0.081 241 MET   BBB C   
3941 O  O   . MET   B 242 ? 0.357 0.125 0.428 0.014  -0.053 -0.072 241 MET   BBB O   
3942 C  CB  . MET   B 242 ? 0.385 0.110 0.515 -0.077 0.031  -0.165 241 MET   BBB CB  
3943 C  CG  . MET   B 242 ? 0.421 0.170 0.631 -0.079 0.078  -0.124 241 MET   BBB CG  
3944 S  SD  . MET   B 242 ? 0.374 0.120 0.535 -0.046 0.028  -0.035 241 MET   BBB SD  
3945 C  CE  . MET   B 242 ? 0.343 0.114 0.479 -0.011 -0.008 -0.129 241 MET   BBB CE  
3946 N  N   . GLN   B 243 ? 0.343 0.099 0.478 0.009  -0.011 -0.096 242 GLN   BBB N   
3947 C  CA  . GLN   B 243 ? 0.428 0.032 0.494 -0.029 -0.003 -0.097 242 GLN   BBB CA  
3948 C  C   . GLN   B 243 ? 0.386 0.026 0.517 -0.082 0.010  -0.035 242 GLN   BBB C   
3949 O  O   . GLN   B 243 ? 0.369 0.014 0.549 -0.050 -0.007 -0.012 242 GLN   BBB O   
3950 C  CB  . GLN   B 243 ? 0.458 0.049 0.563 -0.066 -0.078 -0.103 242 GLN   BBB CB  
3951 C  CG  . GLN   B 243 ? 0.558 0.315 0.584 -0.152 -0.166 -0.122 242 GLN   BBB CG  
3952 C  CD  . GLN   B 243 ? 0.618 0.405 0.670 -0.282 -0.058 -0.058 242 GLN   BBB CD  
3953 O  OE1 . GLN   B 243 ? 0.646 0.718 0.740 -0.296 -0.063 -0.124 242 GLN   BBB OE1 
3954 N  NE2 . GLN   B 243 ? 0.753 0.221 0.714 -0.103 0.045  0.026  242 GLN   BBB NE2 
3955 N  N   . HIS   B 244 ? 0.387 0.008 0.436 -0.011 0.016  -0.020 243 HIS   BBB N   
3956 C  CA  . HIS   B 244 ? 0.347 0.009 0.409 -0.031 0.036  -0.015 243 HIS   BBB CA  
3957 C  C   . HIS   B 244 ? 0.305 0.008 0.353 0.015  -0.010 0.013  243 HIS   BBB C   
3958 O  O   . HIS   B 244 ? 0.357 0.066 0.384 -0.038 -0.002 -0.013 243 HIS   BBB O   
3959 C  CB  . HIS   B 244 ? 0.338 0.008 0.544 -0.007 -0.016 -0.025 243 HIS   BBB CB  
3960 C  CG  . HIS   B 244 ? 0.452 0.068 0.536 -0.049 0.072  -0.115 243 HIS   BBB CG  
3961 N  ND1 . HIS   B 244 ? 0.509 0.088 0.681 0.002  0.068  -0.172 243 HIS   BBB ND1 
3962 C  CD2 . HIS   B 244 ? 0.615 0.088 0.555 0.055  0.020  -0.190 243 HIS   BBB CD2 
3963 C  CE1 . HIS   B 244 ? 0.710 0.098 0.743 -0.034 0.050  -0.194 243 HIS   BBB CE1 
3964 N  NE2 . HIS   B 244 ? 0.767 0.033 0.763 -0.059 0.002  -0.130 243 HIS   BBB NE2 
3965 N  N   . ASN   B 245 ? 0.322 0.011 0.378 0.004  -0.018 -0.043 244 ASN   BBB N   
3966 C  CA  . ASN   B 245 ? 0.309 0.038 0.421 -0.011 -0.012 0.016  244 ASN   BBB CA  
3967 C  C   . ASN   B 245 ? 0.291 0.118 0.395 -0.004 0.026  0.026  244 ASN   BBB C   
3968 O  O   . ASN   B 245 ? 0.341 0.007 0.503 -0.001 0.043  -0.018 244 ASN   BBB O   
3969 C  CB  . ASN   B 245 ? 0.321 0.020 0.390 -0.016 0.007  -0.020 244 ASN   BBB CB  
3970 C  CG  . ASN   B 245 ? 0.307 0.019 0.347 -0.062 0.024  -0.011 244 ASN   BBB CG  
3971 O  OD1 . ASN   B 245 ? 0.331 0.010 0.379 -0.015 0.042  -0.037 244 ASN   BBB OD1 
3972 N  ND2 . ASN   B 245 ? 0.343 0.007 0.391 -0.014 0.015  0.002  244 ASN   BBB ND2 
3973 N  N   . ASN   B 246 ? 0.291 0.016 0.402 -0.044 0.045  -0.038 245 ASN   BBB N   
3974 C  CA  . ASN   B 246 ? 0.320 0.007 0.443 -0.018 -0.017 0.001  245 ASN   BBB CA  
3975 C  C   . ASN   B 246 ? 0.307 0.008 0.476 0.017  -0.032 -0.015 245 ASN   BBB C   
3976 O  O   . ASN   B 246 ? 0.421 0.012 0.539 -0.031 -0.080 -0.039 245 ASN   BBB O   
3977 C  CB  . ASN   B 246 ? 0.345 0.011 0.432 -0.029 -0.009 0.035  245 ASN   BBB CB  
3978 C  CG  . ASN   B 246 ? 0.275 0.010 0.513 0.007  -0.005 0.039  245 ASN   BBB CG  
3979 O  OD1 . ASN   B 246 ? 0.563 0.321 0.548 -0.168 0.039  0.084  245 ASN   BBB OD1 
3980 N  ND2 . ASN   B 246 ? 0.314 0.012 0.525 -0.033 -0.045 0.037  245 ASN   BBB ND2 
3981 N  N   . ARG   B 247 ? 0.321 0.025 0.511 0.067  -0.008 0.045  246 ARG   BBB N   
3982 C  CA  . ARG   B 247 ? 0.347 0.022 0.450 0.071  0.002  -0.019 246 ARG   BBB CA  
3983 C  C   . ARG   B 247 ? 0.366 0.009 0.445 -0.031 0.024  0.006  246 ARG   BBB C   
3984 O  O   . ARG   B 247 ? 0.389 0.015 0.434 -0.059 0.023  -0.005 246 ARG   BBB O   
3985 C  CB  . ARG   B 247 ? 0.339 0.010 0.462 0.032  0.053  0.015  246 ARG   BBB CB  
3986 C  CG  . ARG   B 247 ? 0.297 0.029 0.444 0.082  -0.006 0.009  246 ARG   BBB CG  
3987 C  CD  . ARG   B 247 ? 0.278 0.089 0.467 0.150  0.030  0.012  246 ARG   BBB CD  
3988 N  NE  . ARG   B 247 ? 0.325 0.027 0.532 0.074  0.023  0.048  246 ARG   BBB NE  
3989 C  CZ  . ARG   B 247 ? 0.332 0.031 0.416 0.086  -0.021 -0.037 246 ARG   BBB CZ  
3990 N  NH1 . ARG   B 247 ? 0.312 0.032 0.474 0.021  -0.014 -0.026 246 ARG   BBB NH1 
3991 N  NH2 . ARG   B 247 ? 0.392 0.021 0.600 0.073  0.016  -0.013 246 ARG   BBB NH2 
3992 N  N   . PRO   B 248 ? 0.376 0.009 0.482 -0.031 -0.007 -0.013 247 PRO   BBB N   
3993 C  CA  . PRO   B 248 ? 0.429 0.014 0.479 0.022  0.028  -0.055 247 PRO   BBB CA  
3994 C  C   . PRO   B 248 ? 0.423 0.032 0.496 0.091  0.027  -0.048 247 PRO   BBB C   
3995 O  O   . PRO   B 248 ? 0.403 0.013 0.492 0.013  -0.008 -0.025 247 PRO   BBB O   
3996 C  CB  . PRO   B 248 ? 0.494 0.009 0.511 -0.026 0.020  0.023  247 PRO   BBB CB  
3997 C  CG  . PRO   B 248 ? 0.490 0.007 0.510 -0.003 0.053  0.010  247 PRO   BBB CG  
3998 C  CD  . PRO   B 248 ? 0.514 0.042 0.404 -0.082 0.040  0.074  247 PRO   BBB CD  
3999 N  N   . THR   B 249 ? 0.439 0.007 0.494 0.003  0.038  0.010  248 THR   BBB N   
4000 C  CA  . THR   B 249 ? 0.337 0.008 0.527 0.022  0.109  0.016  248 THR   BBB CA  
4001 C  C   . THR   B 249 ? 0.336 0.027 0.528 0.079  0.070  -0.012 248 THR   BBB C   
4002 O  O   . THR   B 249 ? 0.522 0.039 0.522 -0.013 0.030  0.012  248 THR   BBB O   
4003 C  CB  . THR   B 249 ? 0.349 0.008 0.503 0.000  0.063  0.027  248 THR   BBB CB  
4004 O  OG1 . THR   B 249 ? 0.382 0.016 0.467 -0.050 0.050  0.031  248 THR   BBB OG1 
4005 C  CG2 . THR   B 249 ? 0.360 0.024 0.508 0.051  0.044  -0.005 248 THR   BBB CG2 
4006 N  N   . GLN   B 250 ? 0.384 0.012 0.523 0.010  0.060  0.055  249 GLN   BBB N   
4007 C  CA  . GLN   B 250 ? 0.338 0.064 0.444 0.029  0.038  -0.006 249 GLN   BBB CA  
4008 C  C   . GLN   B 250 ? 0.403 0.106 0.480 0.062  0.028  0.035  249 GLN   BBB C   
4009 O  O   . GLN   B 250 ? 0.475 0.062 0.487 0.005  0.009  0.013  249 GLN   BBB O   
4010 C  CB  . GLN   B 250 ? 0.416 0.018 0.471 0.069  0.053  0.021  249 GLN   BBB CB  
4011 C  CG  . GLN   B 250 ? 0.438 0.107 0.459 -0.003 0.014  0.045  249 GLN   BBB CG  
4012 C  CD  . GLN   B 250 ? 0.461 0.029 0.467 0.071  0.065  -0.008 249 GLN   BBB CD  
4013 O  OE1 . GLN   B 250 ? 0.517 0.045 0.526 0.067  0.079  -0.055 249 GLN   BBB OE1 
4014 N  NE2 . GLN   B 250 ? 0.509 0.011 0.585 0.048  0.038  -0.013 249 GLN   BBB NE2 
4015 N  N   . PRO   B 251 ? 0.460 0.100 0.531 0.083  0.031  0.031  250 PRO   BBB N   
4016 C  CA  . PRO   B 251 ? 0.417 0.172 0.531 0.112  0.010  -0.005 250 PRO   BBB CA  
4017 C  C   . PRO   B 251 ? 0.520 0.042 0.522 0.135  0.056  0.001  250 PRO   BBB C   
4018 O  O   . PRO   B 251 ? 0.473 0.101 0.520 0.045  0.016  0.049  250 PRO   BBB O   
4019 C  CB  . PRO   B 251 ? 0.661 0.048 0.670 0.076  -0.126 0.061  250 PRO   BBB CB  
4020 C  CG  . PRO   B 251 ? 0.663 0.100 0.601 0.177  -0.008 0.020  250 PRO   BBB CG  
4021 C  CD  . PRO   B 251 ? 0.539 0.063 0.592 0.104  -0.046 0.013  250 PRO   BBB CD  
4022 N  N   . LEU   B 252 ? 0.518 0.098 0.533 0.082  0.074  0.103  251 LEU   BBB N   
4023 C  CA  . LEU   B 252 ? 0.547 0.235 0.579 0.032  0.013  0.085  251 LEU   BBB CA  
4024 C  C   . LEU   B 252 ? 0.552 0.009 0.525 0.010  -0.001 -0.013 251 LEU   BBB C   
4025 O  O   . LEU   B 252 ? 0.481 0.089 0.524 0.005  0.010  0.021  251 LEU   BBB O   
4026 C  CB  . LEU   B 252 ? 0.559 0.069 0.616 -0.072 0.025  0.036  251 LEU   BBB CB  
4027 C  CG  . LEU   B 252 ? 0.642 0.115 0.653 -0.079 -0.022 0.025  251 LEU   BBB CG  
4028 C  CD1 . LEU   B 252 ? 0.509 0.285 0.587 0.102  -0.051 0.040  251 LEU   BBB CD1 
4029 C  CD2 . LEU   B 252 ? 0.520 0.366 0.711 -0.053 0.022  0.086  251 LEU   BBB CD2 
4030 N  N   . LYS   B 253 ? 0.611 0.026 0.530 0.072  0.009  -0.019 252 LYS   BBB N   
4031 C  CA  . LYS   B 253 ? 0.592 0.022 0.603 0.087  -0.015 0.039  252 LYS   BBB CA  
4032 C  C   . LYS   B 253 ? 0.560 0.205 0.556 0.087  0.016  -0.009 252 LYS   BBB C   
4033 O  O   . LYS   B 253 ? 0.604 0.338 0.654 0.039  0.094  0.069  252 LYS   BBB O   
4034 C  CB  . LYS   B 253 ? 0.606 0.138 0.659 0.150  -0.054 0.072  252 LYS   BBB CB  
4035 C  CG  . LYS   B 253 ? 0.414 0.186 0.891 0.088  -0.087 0.006  252 LYS   BBB CG  
4036 C  CD  . LYS   B 253 ? 0.686 0.144 0.903 0.046  -0.052 -0.003 252 LYS   BBB CD  
4037 C  CE  . LYS   B 253 ? 0.701 0.411 0.814 0.123  -0.127 -0.050 252 LYS   BBB CE  
4038 N  NZ  . LYS   B 253 ? 0.974 0.448 0.889 0.169  0.022  0.055  252 LYS   BBB NZ  
4039 N  N   . GLY   B 254 ? 0.569 0.049 0.586 0.067  -0.008 0.011  253 GLY   BBB N   
4040 C  CA  . GLY   B 254 ? 0.684 0.093 0.664 0.067  -0.048 0.010  253 GLY   BBB CA  
4041 C  C   . GLY   B 254 ? 0.537 0.109 0.608 0.033  -0.179 0.062  253 GLY   BBB C   
4042 O  O   . GLY   B 254 ? 0.527 0.141 0.496 0.041  -0.101 0.067  253 GLY   BBB O   
4043 N  N   . ARG   B 255 ? 0.560 0.076 0.594 0.092  -0.099 0.022  254 ARG   BBB N   
4044 C  CA  . ARG   B 255 ? 0.487 0.087 0.462 0.052  -0.043 0.018  254 ARG   BBB CA  
4045 C  C   . ARG   B 255 ? 0.402 0.124 0.464 0.023  -0.076 0.012  254 ARG   BBB C   
4046 O  O   . ARG   B 255 ? 0.420 0.060 0.590 0.062  0.008  0.042  254 ARG   BBB O   
4047 C  CB  . ARG   B 255 ? 0.466 0.033 0.481 0.111  0.003  0.009  254 ARG   BBB CB  
4048 C  CG  . ARG   B 255 ? 0.477 0.021 0.485 0.077  0.005  0.032  254 ARG   BBB CG  
4049 C  CD  . ARG   B 255 ? 0.443 0.063 0.438 0.063  0.002  0.062  254 ARG   BBB CD  
4050 N  NE  . ARG   B 255 ? 0.446 0.047 0.551 0.094  -0.037 0.099  254 ARG   BBB NE  
4051 C  CZ  . ARG   B 255 ? 0.359 0.094 0.472 0.062  0.002  0.158  254 ARG   BBB CZ  
4052 N  NH1 . ARG   B 255 ? 0.318 0.048 0.455 0.037  0.000  0.096  254 ARG   BBB NH1 
4053 N  NH2 . ARG   B 255 ? 0.363 0.081 0.489 0.096  -0.003 0.097  254 ARG   BBB NH2 
4054 N  N   . THR   B 256 ? 0.411 0.087 0.485 0.028  -0.062 0.007  255 THR   BBB N   
4055 C  CA  . THR   B 256 ? 0.452 0.079 0.511 0.152  -0.064 0.078  255 THR   BBB CA  
4056 C  C   . THR   B 256 ? 0.411 0.041 0.478 0.101  -0.046 0.056  255 THR   BBB C   
4057 O  O   . THR   B 256 ? 0.386 0.142 0.490 -0.008 -0.046 0.051  255 THR   BBB O   
4058 C  CB  . THR   B 256 ? 0.511 0.217 0.521 0.145  -0.136 0.087  255 THR   BBB CB  
4059 O  OG1 . THR   B 256 ? 0.644 0.306 0.606 0.264  -0.109 0.056  255 THR   BBB OG1 
4060 C  CG2 . THR   B 256 ? 0.690 0.327 0.477 0.102  -0.161 0.061  255 THR   BBB CG2 
4061 N  N   . VAL   B 257 ? 0.395 0.009 0.496 0.025  -0.058 0.021  256 VAL   BBB N   
4062 C  CA  . VAL   B 257 ? 0.317 0.023 0.466 0.042  -0.016 0.069  256 VAL   BBB CA  
4063 C  C   . VAL   B 257 ? 0.311 0.089 0.422 -0.050 -0.002 0.079  256 VAL   BBB C   
4064 O  O   . VAL   B 257 ? 0.395 0.013 0.443 -0.020 -0.019 0.042  256 VAL   BBB O   
4065 C  CB  . VAL   B 257 ? 0.334 0.140 0.422 0.042  -0.027 0.038  256 VAL   BBB CB  
4066 C  CG1 . VAL   B 257 ? 0.328 0.125 0.461 0.028  -0.012 0.075  256 VAL   BBB CG1 
4067 C  CG2 . VAL   B 257 ? 0.390 0.030 0.443 -0.037 -0.081 0.085  256 VAL   BBB CG2 
4068 N  N   . ARG   B 258 ? 0.323 0.060 0.392 -0.026 -0.033 0.085  257 ARG   BBB N   
4069 C  CA  . ARG   B 258 ? 0.306 0.031 0.414 0.041  -0.023 0.061  257 ARG   BBB CA  
4070 C  C   . ARG   B 258 ? 0.353 0.015 0.409 0.023  0.003  0.055  257 ARG   BBB C   
4071 O  O   . ARG   B 258 ? 0.360 0.115 0.424 0.019  -0.016 0.070  257 ARG   BBB O   
4072 C  CB  . ARG   B 258 ? 0.315 0.088 0.410 0.025  -0.019 0.036  257 ARG   BBB CB  
4073 C  CG  . ARG   B 258 ? 0.284 0.168 0.460 0.035  -0.059 0.010  257 ARG   BBB CG  
4074 C  CD  . ARG   B 258 ? 0.308 0.280 0.504 -0.001 -0.047 0.051  257 ARG   BBB CD  
4075 N  NE  . ARG   B 258 ? 0.315 0.195 0.566 -0.018 -0.025 0.103  257 ARG   BBB NE  
4076 C  CZ  . ARG   B 258 ? 0.368 0.163 0.542 0.000  -0.035 0.070  257 ARG   BBB CZ  
4077 N  NH1 . ARG   B 258 ? 0.449 0.265 0.567 -0.011 -0.046 0.025  257 ARG   BBB NH1 
4078 N  NH2 . ARG   B 258 ? 0.450 0.083 0.553 -0.065 -0.083 0.046  257 ARG   BBB NH2 
4079 N  N   . ALA   B 259 ? 0.317 0.014 0.421 0.006  0.000  0.057  258 ALA   BBB N   
4080 C  CA  . ALA   B 259 ? 0.315 0.007 0.462 -0.006 -0.002 0.007  258 ALA   BBB CA  
4081 C  C   . ALA   B 259 ? 0.327 0.021 0.418 -0.023 -0.068 0.077  258 ALA   BBB C   
4082 O  O   . ALA   B 259 ? 0.350 0.019 0.470 -0.017 -0.054 0.056  258 ALA   BBB O   
4083 C  CB  . ALA   B 259 ? 0.345 0.167 0.459 0.013  0.041  0.015  258 ALA   BBB CB  
4084 N  N   . SER   B 260 ? 0.367 0.017 0.404 0.012  -0.053 0.063  259 SER   BBB N   
4085 C  CA  . SER   B 260 ? 0.342 0.083 0.396 -0.041 -0.059 0.026  259 SER   BBB CA  
4086 C  C   . SER   B 260 ? 0.345 0.137 0.350 -0.070 -0.071 0.053  259 SER   BBB C   
4087 O  O   . SER   B 260 ? 0.362 0.102 0.460 -0.062 -0.051 0.004  259 SER   BBB O   
4088 C  CB  . SER   B 260 ? 0.328 0.127 0.404 -0.057 -0.062 0.065  259 SER   BBB CB  
4089 O  OG  . SER   B 260 ? 0.355 0.037 0.465 -0.013 -0.067 0.036  259 SER   BBB OG  
4090 N  N   . PHE   B 261 ? 0.335 0.033 0.479 -0.027 -0.015 -0.005 260 PHE   BBB N   
4091 C  CA  . PHE   B 261 ? 0.382 0.290 0.488 -0.050 -0.005 0.003  260 PHE   BBB CA  
4092 C  C   . PHE   B 261 ? 0.498 0.407 0.454 -0.004 0.052  0.084  260 PHE   BBB C   
4093 O  O   . PHE   B 261 ? 0.563 0.437 0.472 -0.026 0.098  0.052  260 PHE   BBB O   
4094 C  CB  . PHE   B 261 ? 0.445 0.299 0.470 -0.005 -0.036 -0.059 260 PHE   BBB CB  
4095 C  CG  . PHE   B 261 ? 0.311 0.196 0.415 -0.004 -0.034 0.050  260 PHE   BBB CG  
4096 C  CD1 . PHE   B 261 ? 0.335 0.065 0.443 0.036  -0.010 0.037  260 PHE   BBB CD1 
4097 C  CD2 . PHE   B 261 ? 0.404 0.173 0.503 -0.027 0.068  -0.040 260 PHE   BBB CD2 
4098 C  CE1 . PHE   B 261 ? 0.359 0.204 0.455 -0.031 -0.043 0.037  260 PHE   BBB CE1 
4099 C  CE2 . PHE   B 261 ? 0.426 0.184 0.475 -0.055 0.006  0.006  260 PHE   BBB CE2 
4100 C  CZ  . PHE   B 261 ? 0.428 0.106 0.498 -0.007 -0.019 0.082  260 PHE   BBB CZ  
4101 O  OXT . PHE   B 261 ? 0.496 0.322 0.524 -0.069 0.013  0.149  260 PHE   BBB OXT 
4102 C  C   . ACT   C .   ? 0.635 0.322 0.924 -0.068 0.148  -0.032 301 ACT   AAA C   
4103 O  O   . ACT   C .   ? 0.480 0.306 0.733 -0.045 0.027  0.076  301 ACT   AAA O   
4104 O  OXT . ACT   C .   ? 0.542 0.288 0.755 0.056  0.021  -0.068 301 ACT   AAA OXT 
4105 C  CH3 . ACT   C .   ? 0.618 0.219 0.684 -0.082 0.140  0.113  301 ACT   AAA CH3 
4106 C  C   . ACT   D .   ? 0.859 0.525 0.949 -0.186 0.120  -0.315 302 ACT   AAA C   
4107 O  O   . ACT   D .   ? 0.812 0.680 0.894 -0.180 0.018  -0.281 302 ACT   AAA O   
4108 O  OXT . ACT   D .   ? 0.806 0.451 0.810 0.026  0.097  -0.177 302 ACT   AAA OXT 
4109 C  CH3 . ACT   D .   ? 0.773 0.128 0.833 -0.175 0.039  -0.148 302 ACT   AAA CH3 
4110 ZN ZN  . ZN    E .   ? 0.305 0.008 0.427 0.004  0.006  -0.030 303 ZN    AAA ZN  
4111 C  C2  . A1H6C F .   ? 0.530 0.365 0.735 0.131  0.061  -0.105 304 A1H6C AAA C2  
4112 C  C3  . A1H6C F .   ? 0.654 0.039 0.653 0.072  0.068  0.018  304 A1H6C AAA C3  
4113 C  C4  . A1H6C F .   ? 0.669 0.176 0.716 0.083  0.010  -0.008 304 A1H6C AAA C4  
4114 C  C6  . A1H6C F .   ? 0.744 0.180 0.751 0.008  -0.240 -0.105 304 A1H6C AAA C6  
4115 C  C7  . A1H6C F .   ? 0.564 0.730 0.785 -0.031 -0.301 -0.125 304 A1H6C AAA C7  
4116 C  C8  . A1H6C F .   ? 0.600 0.821 0.729 0.060  -0.163 -0.130 304 A1H6C AAA C8  
4117 C  C9  . A1H6C F .   ? 0.734 0.648 0.719 0.251  -0.210 0.058  304 A1H6C AAA C9  
4118 C  C10 . A1H6C F .   ? 0.700 0.646 0.794 0.145  -0.019 0.286  304 A1H6C AAA C10 
4119 C  C11 . A1H6C F .   ? 0.637 0.561 0.818 0.110  -0.259 -0.031 304 A1H6C AAA C11 
4120 C  C12 . A1H6C F .   ? 0.637 0.375 0.739 -0.089 -0.179 -0.156 304 A1H6C AAA C12 
4121 C  C14 . A1H6C F .   ? 0.405 0.426 0.441 0.019  -0.035 -0.095 304 A1H6C AAA C14 
4122 C  C15 . A1H6C F .   ? 0.360 0.467 0.438 0.072  0.046  -0.103 304 A1H6C AAA C15 
4123 C  C16 . A1H6C F .   ? 0.351 0.282 0.369 0.016  0.045  -0.047 304 A1H6C AAA C16 
4124 C  C17 . A1H6C F .   ? 0.302 0.265 0.376 0.009  -0.019 -0.049 304 A1H6C AAA C17 
4125 O  O1  . A1H6C F .   ? 0.664 0.278 0.777 0.116  -0.018 -0.017 304 A1H6C AAA O1  
4126 S  S5  . A1H6C F .   ? 0.662 0.187 0.731 0.054  -0.104 -0.104 304 A1H6C AAA S5  
4127 O  O13 . A1H6C F .   ? 0.456 0.663 0.642 0.116  0.016  -0.239 304 A1H6C AAA O13 
4128 S  S18 . A1H6C F .   ? 0.268 0.052 0.410 -0.028 0.004  -0.023 304 A1H6C AAA S18 
4129 O  O19 . A1H6C F .   ? 0.304 0.148 0.403 0.025  0.045  0.026  304 A1H6C AAA O19 
4130 N  N20 . A1H6C F .   ? 0.262 0.064 0.368 -0.014 -0.024 -0.058 304 A1H6C AAA N20 
4131 O  O21 . A1H6C F .   ? 0.268 0.070 0.452 -0.037 0.011  -0.056 304 A1H6C AAA O21 
4132 C  C22 . A1H6C F .   ? 0.355 0.204 0.443 -0.000 0.029  -0.024 304 A1H6C AAA C22 
4133 C  C23 . A1H6C F .   ? 0.382 0.191 0.475 0.119  -0.033 -0.102 304 A1H6C AAA C23 
4134 ZN ZN  . ZN    G .   ? 0.322 0.007 0.475 -0.007 -0.010 0.014  301 ZN    BBB ZN  
4135 C  C2  . A1H6C H .   ? 0.670 0.824 0.872 -0.106 0.126  0.161  302 A1H6C BBB C2  
4136 C  C3  . A1H6C H .   ? 0.899 0.665 0.899 -0.104 0.218  0.155  302 A1H6C BBB C3  
4137 C  C4  . A1H6C H .   ? 0.803 0.484 0.985 0.139  0.198  0.263  302 A1H6C BBB C4  
4138 C  C6  . A1H6C H .   ? 1.196 0.321 0.797 -0.002 0.024  0.134  302 A1H6C BBB C6  
4139 C  C7  . A1H6C H .   ? 1.113 0.649 0.625 -0.152 -0.073 0.244  302 A1H6C BBB C7  
4140 C  C8  . A1H6C H .   ? 0.559 0.441 0.646 -0.024 -0.042 0.056  302 A1H6C BBB C8  
4141 C  C9  . A1H6C H .   ? 0.678 0.397 0.662 -0.070 -0.013 0.045  302 A1H6C BBB C9  
4142 C  C10 . A1H6C H .   ? 0.516 0.330 0.703 0.153  0.096  0.057  302 A1H6C BBB C10 
4143 C  C11 . A1H6C H .   ? 1.034 0.348 0.731 -0.092 0.021  -0.120 302 A1H6C BBB C11 
4144 C  C12 . A1H6C H .   ? 1.219 0.285 0.830 0.118  0.036  0.086  302 A1H6C BBB C12 
4145 C  C14 . A1H6C H .   ? 0.702 0.332 0.728 -0.047 -0.032 0.300  302 A1H6C BBB C14 
4146 C  C15 . A1H6C H .   ? 0.395 0.487 0.665 -0.209 -0.056 0.256  302 A1H6C BBB C15 
4147 C  C16 . A1H6C H .   ? 0.407 0.339 0.599 -0.126 -0.076 0.170  302 A1H6C BBB C16 
4148 C  C17 . A1H6C H .   ? 0.322 0.243 0.484 -0.028 -0.004 0.035  302 A1H6C BBB C17 
4149 O  O1  . A1H6C H .   ? 0.960 0.695 0.965 -0.228 -0.162 0.119  302 A1H6C BBB O1  
4150 S  S5  . A1H6C H .   ? 0.696 0.532 1.027 -0.114 -0.121 0.243  302 A1H6C BBB S5  
4151 O  O13 . A1H6C H .   ? 0.663 0.810 0.819 -0.163 -0.021 0.353  302 A1H6C BBB O13 
4152 S  S18 . A1H6C H .   ? 0.272 0.051 0.437 0.054  -0.030 0.012  302 A1H6C BBB S18 
4153 O  O19 . A1H6C H .   ? 0.217 0.043 0.434 0.033  -0.028 0.000  302 A1H6C BBB O19 
4154 N  N20 . A1H6C H .   ? 0.229 0.089 0.408 0.071  -0.031 0.029  302 A1H6C BBB N20 
4155 O  O21 . A1H6C H .   ? 0.338 0.008 0.532 -0.021 -0.015 -0.005 302 A1H6C BBB O21 
4156 C  C22 . A1H6C H .   ? 0.376 0.309 0.479 -0.125 0.021  0.097  302 A1H6C BBB C22 
4157 C  C23 . A1H6C H .   ? 0.409 0.533 0.519 -0.121 0.001  0.218  302 A1H6C BBB C23 
4158 O  O   . HOH   I .   ? 0.321 0.586 0.504 0.021  -0.015 0.289  401 HOH   AAA O   
4159 O  O   . HOH   I .   ? 0.691 0.417 0.792 0.102  0.123  0.138  402 HOH   AAA O   
4160 O  O   . HOH   I .   ? 1.401 0.204 0.815 0.176  -0.120 -0.099 403 HOH   AAA O   
4161 O  O   . HOH   I .   ? 0.491 0.342 0.482 -0.115 0.021  -0.091 404 HOH   AAA O   
4162 O  O   . HOH   I .   ? 0.534 0.297 0.550 -0.082 -0.018 0.077  405 HOH   AAA O   
4163 O  O   . HOH   I .   ? 0.552 0.681 0.579 -0.142 -0.057 -0.057 406 HOH   AAA O   
4164 O  O   . HOH   I .   ? 0.354 0.106 0.499 -0.086 -0.041 -0.024 407 HOH   AAA O   
4165 O  O   . HOH   I .   ? 0.561 0.303 0.715 0.018  0.007  -0.055 408 HOH   AAA O   
4166 O  O   . HOH   I .   ? 0.613 0.124 0.538 0.042  -0.061 -0.019 409 HOH   AAA O   
4167 O  O   . HOH   I .   ? 0.606 0.309 0.694 0.171  -0.076 0.097  410 HOH   AAA O   
4168 O  O   . HOH   I .   ? 0.334 0.492 0.456 0.106  -0.026 -0.042 411 HOH   AAA O   
4169 O  O   . HOH   I .   ? 0.420 0.010 0.498 -0.011 0.019  -0.043 412 HOH   AAA O   
4170 O  O   . HOH   I .   ? 1.170 0.296 0.632 0.126  -0.110 -0.054 413 HOH   AAA O   
4171 O  O   . HOH   I .   ? 0.349 0.008 0.415 0.008  0.004  -0.027 414 HOH   AAA O   
4172 O  O   . HOH   I .   ? 0.534 0.471 0.575 -0.065 0.077  0.045  415 HOH   AAA O   
4173 O  O   . HOH   I .   ? 0.605 0.799 0.954 0.110  -0.139 -0.484 416 HOH   AAA O   
4174 O  O   . HOH   I .   ? 0.472 0.284 0.561 0.004  -0.036 -0.101 417 HOH   AAA O   
4175 O  O   . HOH   I .   ? 0.618 0.367 0.667 0.209  -0.010 -0.010 418 HOH   AAA O   
4176 O  O   . HOH   I .   ? 0.598 0.185 0.757 0.085  -0.009 -0.030 419 HOH   AAA O   
4177 O  O   . HOH   I .   ? 0.840 0.185 0.762 -0.047 -0.098 -0.170 420 HOH   AAA O   
4178 O  O   . HOH   I .   ? 0.918 0.311 0.575 -0.099 -0.014 -0.010 421 HOH   AAA O   
4179 O  O   . HOH   I .   ? 0.616 0.444 0.726 0.008  -0.024 -0.214 422 HOH   AAA O   
4180 O  O   . HOH   I .   ? 0.407 0.181 0.528 -0.055 0.098  -0.108 423 HOH   AAA O   
4181 O  O   . HOH   I .   ? 0.443 0.124 0.784 -0.053 0.042  -0.060 424 HOH   AAA O   
4182 O  O   . HOH   I .   ? 0.517 0.503 0.583 0.092  0.085  -0.178 425 HOH   AAA O   
4183 O  O   . HOH   I .   ? 0.619 0.159 0.538 0.077  0.025  0.063  426 HOH   AAA O   
4184 O  O   . HOH   I .   ? 0.374 0.057 0.521 0.010  0.064  -0.019 427 HOH   AAA O   
4185 O  O   . HOH   I .   ? 0.570 0.364 0.604 0.061  0.050  0.043  428 HOH   AAA O   
4186 O  O   . HOH   I .   ? 0.733 0.680 0.520 0.298  -0.068 -0.093 429 HOH   AAA O   
4187 O  O   . HOH   I .   ? 0.398 0.016 0.481 -0.006 0.002  -0.014 430 HOH   AAA O   
4188 O  O   . HOH   I .   ? 0.547 0.056 0.729 -0.048 0.041  0.051  431 HOH   AAA O   
4189 O  O   . HOH   I .   ? 0.518 0.029 0.608 -0.034 0.038  -0.007 432 HOH   AAA O   
4190 O  O   . HOH   I .   ? 0.356 0.283 0.506 0.012  0.019  0.003  433 HOH   AAA O   
4191 O  O   . HOH   I .   ? 0.426 0.161 0.584 0.042  0.052  0.001  434 HOH   AAA O   
4192 O  O   . HOH   I .   ? 0.340 0.098 0.456 0.006  -0.009 0.022  435 HOH   AAA O   
4193 O  O   . HOH   I .   ? 0.590 0.130 0.560 0.066  -0.000 0.006  436 HOH   AAA O   
4194 O  O   . HOH   I .   ? 0.523 0.052 0.638 0.061  -0.001 0.037  437 HOH   AAA O   
4195 O  O   . HOH   I .   ? 0.631 0.223 0.630 0.078  0.005  -0.080 438 HOH   AAA O   
4196 O  O   . HOH   I .   ? 0.462 0.209 0.636 0.000  0.055  0.011  439 HOH   AAA O   
4197 O  O   . HOH   I .   ? 0.461 0.271 0.794 0.036  0.103  -0.088 440 HOH   AAA O   
4198 O  O   . HOH   I .   ? 0.539 0.370 0.553 0.039  0.030  0.052  441 HOH   AAA O   
4199 O  O   . HOH   I .   ? 0.547 0.209 0.574 -0.093 0.006  0.007  442 HOH   AAA O   
4200 O  O   . HOH   I .   ? 0.519 0.149 0.591 -0.011 0.055  -0.015 443 HOH   AAA O   
4201 O  O   . HOH   I .   ? 0.437 0.183 0.535 0.018  -0.017 -0.023 444 HOH   AAA O   
4202 O  O   . HOH   I .   ? 0.802 0.323 0.623 0.078  0.107  -0.056 445 HOH   AAA O   
4203 O  O   . HOH   I .   ? 0.708 0.202 0.635 0.111  0.148  -0.013 446 HOH   AAA O   
4204 O  O   . HOH   I .   ? 0.340 0.245 0.561 -0.008 -0.022 -0.043 447 HOH   AAA O   
4205 O  O   . HOH   I .   ? 0.508 0.359 0.700 -0.178 0.056  -0.029 448 HOH   AAA O   
4206 O  O   . HOH   I .   ? 0.403 0.087 0.480 0.055  -0.009 -0.011 449 HOH   AAA O   
4207 O  O   . HOH   I .   ? 0.711 0.180 0.597 -0.127 0.032  0.047  450 HOH   AAA O   
4208 O  O   . HOH   I .   ? 0.317 0.310 0.470 0.063  0.036  -0.071 451 HOH   AAA O   
4209 O  O   . HOH   I .   ? 0.861 0.157 0.596 0.076  0.053  -0.042 452 HOH   AAA O   
4210 O  O   . HOH   I .   ? 0.530 0.244 0.739 -0.054 0.216  -0.161 453 HOH   AAA O   
4211 O  O   . HOH   I .   ? 0.556 0.143 0.604 0.016  0.042  0.026  454 HOH   AAA O   
4212 O  O   . HOH   I .   ? 0.527 0.188 0.687 -0.003 0.109  -0.035 455 HOH   AAA O   
4213 O  O   . HOH   I .   ? 0.479 0.216 0.662 0.067  0.047  -0.003 456 HOH   AAA O   
4214 O  O   . HOH   I .   ? 0.482 0.121 0.574 -0.093 0.079  -0.091 457 HOH   AAA O   
4215 O  O   . HOH   I .   ? 0.458 0.227 0.724 -0.055 0.026  -0.090 458 HOH   AAA O   
4216 O  O   . HOH   I .   ? 0.346 0.121 0.535 0.027  -0.056 0.029  459 HOH   AAA O   
4217 O  O   . HOH   I .   ? 0.594 0.428 0.701 0.065  0.045  0.128  460 HOH   AAA O   
4218 O  O   . HOH   I .   ? 0.417 0.080 0.487 0.064  0.022  -0.030 461 HOH   AAA O   
4219 O  O   . HOH   I .   ? 0.661 0.537 0.979 -0.049 -0.268 0.120  462 HOH   AAA O   
4220 O  O   . HOH   I .   ? 0.499 0.539 0.720 -0.146 0.120  -0.074 463 HOH   AAA O   
4221 O  O   . HOH   I .   ? 0.437 0.012 0.508 0.046  0.048  -0.011 464 HOH   AAA O   
4222 O  O   . HOH   I .   ? 0.442 0.101 0.677 0.005  0.077  -0.041 465 HOH   AAA O   
4223 O  O   . HOH   I .   ? 0.431 0.304 0.620 -0.059 -0.065 -0.122 466 HOH   AAA O   
4224 O  O   . HOH   I .   ? 0.429 0.107 0.511 -0.014 0.036  -0.054 467 HOH   AAA O   
4225 O  O   . HOH   I .   ? 0.490 0.221 0.653 -0.033 0.156  -0.153 468 HOH   AAA O   
4226 O  O   . HOH   I .   ? 0.314 0.168 0.425 -0.024 0.009  -0.049 469 HOH   AAA O   
4227 O  O   . HOH   I .   ? 0.479 0.201 0.652 -0.145 0.059  -0.111 470 HOH   AAA O   
4228 O  O   . HOH   I .   ? 0.609 0.200 0.667 0.049  0.038  0.004  471 HOH   AAA O   
4229 O  O   . HOH   I .   ? 0.432 0.022 0.534 0.018  0.039  0.020  472 HOH   AAA O   
4230 O  O   . HOH   I .   ? 0.475 0.073 0.508 -0.076 0.052  -0.060 473 HOH   AAA O   
4231 O  O   . HOH   I .   ? 0.377 0.071 0.558 -0.026 0.058  -0.073 474 HOH   AAA O   
4232 O  O   . HOH   I .   ? 0.483 0.082 0.537 0.023  0.028  0.018  475 HOH   AAA O   
4233 O  O   . HOH   I .   ? 0.419 0.008 0.507 0.002  -0.043 -0.026 476 HOH   AAA O   
4234 O  O   . HOH   I .   ? 0.359 0.029 0.478 0.044  0.037  -0.023 477 HOH   AAA O   
4235 O  O   . HOH   I .   ? 0.471 0.226 0.685 0.078  -0.049 -0.038 478 HOH   AAA O   
4236 O  O   . HOH   I .   ? 0.532 0.347 0.744 -0.109 0.059  -0.045 479 HOH   AAA O   
4237 O  O   . HOH   I .   ? 0.335 0.012 0.412 0.042  -0.039 0.003  480 HOH   AAA O   
4238 O  O   . HOH   I .   ? 0.434 0.120 0.452 -0.055 0.038  -0.037 481 HOH   AAA O   
4239 O  O   . HOH   I .   ? 0.327 0.006 0.520 0.002  0.028  -0.007 482 HOH   AAA O   
4240 O  O   . HOH   I .   ? 0.319 0.058 0.401 -0.017 0.016  -0.044 483 HOH   AAA O   
4241 O  O   . HOH   I .   ? 0.295 0.598 0.331 -0.080 -0.041 -0.031 484 HOH   AAA O   
4242 O  O   . HOH   I .   ? 0.382 0.402 0.458 0.011  -0.016 -0.119 485 HOH   AAA O   
4243 O  O   . HOH   I .   ? 0.360 0.259 0.556 -0.014 -0.040 -0.108 486 HOH   AAA O   
4244 O  O   . HOH   I .   ? 0.603 0.394 0.851 -0.042 0.033  -0.345 487 HOH   AAA O   
4245 O  O   . HOH   I .   ? 0.352 0.120 0.476 0.033  -0.024 -0.066 488 HOH   AAA O   
4246 O  O   . HOH   I .   ? 0.587 0.281 0.515 -0.033 0.065  -0.137 489 HOH   AAA O   
4247 O  O   . HOH   I .   ? 1.165 0.764 0.492 -0.137 -0.090 0.121  490 HOH   AAA O   
4248 O  O   . HOH   I .   ? 0.273 0.238 0.531 0.075  0.052  0.069  491 HOH   AAA O   
4249 O  O   . HOH   I .   ? 0.359 0.165 0.487 -0.068 0.018  -0.038 492 HOH   AAA O   
4250 O  O   . HOH   I .   ? 0.520 0.290 0.895 0.024  0.049  -0.050 493 HOH   AAA O   
4251 O  O   . HOH   I .   ? 0.467 0.124 0.542 -0.026 0.016  0.010  494 HOH   AAA O   
4252 O  O   . HOH   I .   ? 0.522 0.416 0.722 -0.047 0.018  -0.018 495 HOH   AAA O   
4253 O  O   . HOH   I .   ? 0.639 0.294 0.936 -0.171 -0.111 0.142  496 HOH   AAA O   
4254 O  O   . HOH   I .   ? 0.361 0.085 0.461 0.011  -0.020 -0.021 497 HOH   AAA O   
4255 O  O   . HOH   I .   ? 0.335 0.427 0.540 0.073  -0.015 0.083  498 HOH   AAA O   
4256 O  O   . HOH   I .   ? 0.653 0.146 0.535 0.052  0.042  0.045  499 HOH   AAA O   
4257 O  O   . HOH   I .   ? 0.608 0.197 0.649 -0.090 0.173  -0.025 500 HOH   AAA O   
4258 O  O   . HOH   I .   ? 0.547 0.144 0.592 0.013  0.023  0.057  501 HOH   AAA O   
4259 O  O   . HOH   I .   ? 0.501 0.094 0.488 0.034  0.029  -0.024 502 HOH   AAA O   
4260 O  O   . HOH   I .   ? 0.414 0.110 0.541 0.052  -0.013 -0.072 503 HOH   AAA O   
4261 O  O   . HOH   I .   ? 0.422 0.119 0.644 0.049  0.009  -0.120 504 HOH   AAA O   
4262 O  O   . HOH   I .   ? 0.669 0.394 0.592 0.305  -0.024 -0.063 505 HOH   AAA O   
4263 O  O   . HOH   I .   ? 1.253 0.229 0.554 -0.012 0.318  -0.027 506 HOH   AAA O   
4264 O  O   . HOH   I .   ? 0.467 0.113 0.553 -0.084 0.048  -0.135 507 HOH   AAA O   
4265 O  O   . HOH   I .   ? 0.517 0.224 0.524 -0.147 -0.013 -0.038 508 HOH   AAA O   
4266 O  O   . HOH   I .   ? 0.341 0.037 0.436 0.042  -0.007 0.004  509 HOH   AAA O   
4267 O  O   . HOH   I .   ? 0.417 0.419 0.509 -0.082 0.041  -0.060 510 HOH   AAA O   
4268 O  O   . HOH   I .   ? 0.652 0.148 0.650 -0.006 -0.054 -0.046 511 HOH   AAA O   
4269 O  O   . HOH   I .   ? 0.540 0.288 0.617 -0.107 0.053  -0.055 512 HOH   AAA O   
4270 O  O   . HOH   I .   ? 0.513 0.227 0.841 0.032  -0.066 -0.028 513 HOH   AAA O   
4271 O  O   . HOH   I .   ? 0.352 0.026 0.476 0.031  -0.039 -0.049 514 HOH   AAA O   
4272 O  O   . HOH   I .   ? 0.493 0.136 0.824 -0.032 0.133  0.071  515 HOH   AAA O   
4273 O  O   . HOH   I .   ? 0.356 0.226 0.539 0.049  -0.012 -0.060 516 HOH   AAA O   
4274 O  O   . HOH   I .   ? 0.474 0.191 0.490 0.073  0.033  0.005  517 HOH   AAA O   
4275 O  O   . HOH   I .   ? 0.448 0.369 0.651 0.006  0.071  -0.203 518 HOH   AAA O   
4276 O  O   . HOH   I .   ? 0.503 0.231 0.576 -0.048 0.157  -0.030 519 HOH   AAA O   
4277 O  O   . HOH   I .   ? 0.362 0.182 0.613 -0.026 0.016  -0.050 520 HOH   AAA O   
4278 O  O   . HOH   I .   ? 0.450 0.334 0.728 0.010  -0.112 -0.225 521 HOH   AAA O   
4279 O  O   . HOH   I .   ? 0.486 0.289 0.702 0.033  -0.048 -0.141 522 HOH   AAA O   
4280 O  O   . HOH   I .   ? 0.454 0.131 0.575 -0.023 0.030  -0.080 523 HOH   AAA O   
4281 O  O   . HOH   I .   ? 0.925 0.306 0.493 0.001  -0.034 0.067  524 HOH   AAA O   
4282 O  O   . HOH   I .   ? 0.450 0.176 0.441 0.043  0.033  0.004  525 HOH   AAA O   
4283 O  O   . HOH   I .   ? 0.477 0.566 0.765 -0.144 -0.088 0.222  526 HOH   AAA O   
4284 O  O   . HOH   I .   ? 0.443 0.491 0.469 -0.100 -0.013 -0.123 527 HOH   AAA O   
4285 O  O   . HOH   I .   ? 0.411 0.147 0.541 0.030  -0.004 -0.052 528 HOH   AAA O   
4286 O  O   . HOH   I .   ? 0.583 0.162 0.615 0.004  0.120  -0.045 529 HOH   AAA O   
4287 O  O   . HOH   I .   ? 1.289 0.590 0.424 -0.086 0.036  -0.041 530 HOH   AAA O   
4288 O  O   . HOH   I .   ? 0.580 0.301 0.638 -0.035 -0.000 -0.018 531 HOH   AAA O   
4289 O  O   . HOH   I .   ? 0.526 0.626 0.865 0.129  0.246  0.008  532 HOH   AAA O   
4290 O  O   . HOH   I .   ? 0.497 0.400 0.541 0.033  -0.025 -0.104 533 HOH   AAA O   
4291 O  O   . HOH   I .   ? 0.608 0.192 0.816 0.044  0.061  -0.066 534 HOH   AAA O   
4292 O  O   . HOH   I .   ? 0.617 0.090 0.506 0.088  0.043  -0.025 535 HOH   AAA O   
4293 O  O   . HOH   I .   ? 0.496 0.054 0.715 -0.122 0.034  -0.017 536 HOH   AAA O   
4294 O  O   . HOH   I .   ? 0.827 0.352 0.733 -0.077 0.088  -0.021 537 HOH   AAA O   
4295 O  O   . HOH   I .   ? 0.497 0.201 0.585 0.050  -0.001 -0.071 538 HOH   AAA O   
4296 O  O   . HOH   I .   ? 0.575 0.160 0.590 -0.072 0.004  -0.065 539 HOH   AAA O   
4297 O  O   . HOH   I .   ? 0.391 0.124 0.535 0.044  -0.020 -0.098 540 HOH   AAA O   
4298 O  O   . HOH   I .   ? 0.464 0.122 0.478 -0.041 0.071  -0.063 541 HOH   AAA O   
4299 O  O   . HOH   I .   ? 0.475 0.171 0.596 -0.062 -0.102 0.083  542 HOH   AAA O   
4300 O  O   . HOH   I .   ? 0.518 0.168 0.543 0.122  -0.015 -0.103 543 HOH   AAA O   
4301 O  O   . HOH   I .   ? 0.455 0.288 0.662 0.047  -0.043 0.100  544 HOH   AAA O   
4302 O  O   . HOH   I .   ? 0.606 0.428 0.477 -0.007 -0.010 0.077  545 HOH   AAA O   
4303 O  O   . HOH   I .   ? 0.365 0.159 0.541 -0.014 0.015  0.052  546 HOH   AAA O   
4304 O  O   . HOH   I .   ? 0.525 0.194 0.462 -0.179 0.015  0.014  547 HOH   AAA O   
4305 O  O   . HOH   I .   ? 0.459 0.608 0.693 0.077  -0.000 0.115  548 HOH   AAA O   
4306 O  O   . HOH   I .   ? 0.508 0.210 0.649 -0.057 0.076  -0.003 549 HOH   AAA O   
4307 O  O   . HOH   I .   ? 0.385 0.145 0.543 0.064  0.020  -0.051 550 HOH   AAA O   
4308 O  O   . HOH   I .   ? 0.572 0.168 0.566 0.040  0.081  -0.041 551 HOH   AAA O   
4309 O  O   . HOH   I .   ? 0.636 0.200 0.731 0.044  -0.004 0.119  552 HOH   AAA O   
4310 O  O   . HOH   I .   ? 0.430 0.140 0.426 0.011  0.004  -0.017 553 HOH   AAA O   
4311 O  O   . HOH   I .   ? 0.621 0.133 0.770 0.034  -0.065 -0.103 554 HOH   AAA O   
4312 O  O   . HOH   I .   ? 0.598 0.228 0.720 -0.073 -0.026 -0.006 555 HOH   AAA O   
4313 O  O   . HOH   I .   ? 0.843 0.273 0.598 0.057  0.107  -0.114 556 HOH   AAA O   
4314 O  O   . HOH   I .   ? 0.415 0.149 0.527 -0.117 0.069  -0.043 557 HOH   AAA O   
4315 O  O   . HOH   I .   ? 0.392 0.188 0.647 -0.067 0.005  -0.089 558 HOH   AAA O   
4316 O  O   . HOH   I .   ? 0.424 0.283 0.643 0.069  -0.052 -0.119 559 HOH   AAA O   
4317 O  O   . HOH   I .   ? 0.777 0.239 0.617 0.122  0.136  0.074  560 HOH   AAA O   
4318 O  O   . HOH   I .   ? 0.383 0.416 0.570 -0.005 -0.019 -0.056 561 HOH   AAA O   
4319 O  O   . HOH   I .   ? 0.799 0.313 0.649 0.107  0.168  0.142  562 HOH   AAA O   
4320 O  O   . HOH   I .   ? 0.621 0.481 0.992 0.056  -0.011 -0.023 563 HOH   AAA O   
4321 O  O   . HOH   I .   ? 0.652 0.286 0.648 -0.043 0.013  -0.006 564 HOH   AAA O   
4322 O  O   . HOH   I .   ? 0.660 0.409 0.600 -0.132 -0.030 -0.141 565 HOH   AAA O   
4323 O  O   . HOH   I .   ? 0.438 0.149 0.680 -0.031 -0.008 -0.033 566 HOH   AAA O   
4324 O  O   . HOH   I .   ? 0.516 0.099 0.875 -0.009 -0.004 -0.051 567 HOH   AAA O   
4325 O  O   . HOH   I .   ? 0.505 0.259 0.658 -0.017 0.003  -0.178 568 HOH   AAA O   
4326 O  O   . HOH   I .   ? 0.527 0.294 0.724 -0.062 0.125  -0.096 569 HOH   AAA O   
4327 O  O   . HOH   I .   ? 0.648 0.252 0.662 -0.119 -0.020 -0.148 570 HOH   AAA O   
4328 O  O   . HOH   I .   ? 0.441 0.151 0.593 -0.109 0.130  -0.090 571 HOH   AAA O   
4329 O  O   . HOH   I .   ? 0.498 0.361 0.422 0.210  -0.017 0.006  572 HOH   AAA O   
4330 O  O   . HOH   I .   ? 0.452 0.191 0.520 0.103  -0.018 0.008  573 HOH   AAA O   
4331 O  O   . HOH   I .   ? 0.844 0.261 0.749 -0.017 0.052  -0.009 574 HOH   AAA O   
4332 O  O   . HOH   I .   ? 0.868 0.122 0.769 0.169  -0.092 -0.110 575 HOH   AAA O   
4333 O  O   . HOH   I .   ? 0.543 0.157 0.645 -0.069 0.083  -0.061 576 HOH   AAA O   
4334 O  O   . HOH   I .   ? 0.453 0.215 0.920 0.010  0.079  -0.102 577 HOH   AAA O   
4335 O  O   . HOH   I .   ? 0.986 0.225 0.668 -0.039 -0.094 0.007  578 HOH   AAA O   
4336 O  O   . HOH   I .   ? 0.525 0.546 0.759 0.099  -0.027 -0.014 579 HOH   AAA O   
4337 O  O   . HOH   I .   ? 0.527 0.648 0.933 0.175  0.074  0.279  580 HOH   AAA O   
4338 O  O   . HOH   I .   ? 1.456 0.966 0.572 -0.536 0.018  -0.117 581 HOH   AAA O   
4339 O  O   . HOH   I .   ? 0.542 0.450 0.934 0.047  0.183  0.052  582 HOH   AAA O   
4340 O  O   . HOH   I .   ? 0.554 0.123 0.622 0.054  0.090  -0.039 583 HOH   AAA O   
4341 O  O   . HOH   I .   ? 0.563 0.188 0.692 -0.177 -0.021 -0.045 584 HOH   AAA O   
4342 O  O   . HOH   I .   ? 0.614 0.259 0.680 0.093  -0.127 -0.148 585 HOH   AAA O   
4343 O  O   . HOH   I .   ? 0.529 0.525 0.533 0.048  -0.056 -0.155 586 HOH   AAA O   
4344 O  O   . HOH   I .   ? 0.496 0.331 0.527 -0.098 0.002  -0.136 587 HOH   AAA O   
4345 O  O   . HOH   I .   ? 0.582 0.660 0.620 0.093  -0.022 -0.238 588 HOH   AAA O   
4346 O  O   . HOH   I .   ? 0.658 0.219 0.551 0.093  -0.015 -0.016 589 HOH   AAA O   
4347 O  O   . HOH   I .   ? 0.520 0.326 0.786 -0.042 -0.106 -0.006 590 HOH   AAA O   
4348 O  O   . HOH   I .   ? 0.390 0.140 0.543 -0.024 0.061  -0.029 591 HOH   AAA O   
4349 O  O   . HOH   I .   ? 0.577 0.299 0.855 -0.002 -0.119 -0.012 592 HOH   AAA O   
4350 O  O   . HOH   I .   ? 0.694 0.525 0.536 -0.149 0.008  -0.112 593 HOH   AAA O   
4351 O  O   . HOH   I .   ? 0.425 0.356 0.919 0.087  0.186  0.078  594 HOH   AAA O   
4352 O  O   . HOH   I .   ? 0.401 0.114 0.430 0.063  -0.040 0.021  595 HOH   AAA O   
4353 O  O   . HOH   I .   ? 0.456 0.457 0.722 0.037  0.006  -0.029 596 HOH   AAA O   
4354 O  O   . HOH   I .   ? 0.521 0.615 0.977 -0.022 0.158  -0.446 597 HOH   AAA O   
4355 O  O   . HOH   I .   ? 0.576 0.384 0.717 0.005  0.054  -0.159 598 HOH   AAA O   
4356 O  O   . HOH   I .   ? 0.872 0.593 0.623 0.131  0.026  0.014  599 HOH   AAA O   
4357 O  O   . HOH   I .   ? 0.492 0.186 0.509 0.043  -0.059 0.014  600 HOH   AAA O   
4358 O  O   . HOH   I .   ? 0.670 0.332 0.726 -0.015 0.096  0.106  601 HOH   AAA O   
4359 O  O   . HOH   I .   ? 0.622 0.220 0.568 -0.101 0.034  -0.084 602 HOH   AAA O   
4360 O  O   . HOH   I .   ? 0.593 0.266 0.618 -0.130 -0.116 0.063  603 HOH   AAA O   
4361 O  O   . HOH   I .   ? 0.551 0.342 0.702 -0.059 -0.071 -0.153 604 HOH   AAA O   
4362 O  O   . HOH   I .   ? 0.726 0.200 0.594 -0.003 0.036  -0.022 605 HOH   AAA O   
4363 O  O   . HOH   I .   ? 0.448 0.174 0.500 -0.020 0.049  0.018  606 HOH   AAA O   
4364 O  O   . HOH   I .   ? 0.494 0.937 0.700 0.102  0.170  0.164  607 HOH   AAA O   
4365 O  O   . HOH   I .   ? 0.674 0.242 0.475 0.046  0.046  -0.122 608 HOH   AAA O   
4366 O  O   . HOH   I .   ? 0.433 0.175 0.731 -0.042 0.033  -0.011 609 HOH   AAA O   
4367 O  O   . HOH   I .   ? 0.674 0.492 0.762 -0.141 0.043  -0.241 610 HOH   AAA O   
4368 O  O   . HOH   I .   ? 0.644 0.183 0.628 -0.048 0.043  -0.103 611 HOH   AAA O   
4369 O  O   . HOH   I .   ? 0.565 0.362 0.780 0.075  0.063  0.122  612 HOH   AAA O   
4370 O  O   . HOH   I .   ? 0.516 0.844 0.569 -0.194 0.043  0.111  613 HOH   AAA O   
4371 O  O   . HOH   I .   ? 0.553 0.086 0.783 0.083  0.004  -0.087 614 HOH   AAA O   
4372 O  O   . HOH   I .   ? 0.572 0.363 0.534 0.169  0.090  0.002  615 HOH   AAA O   
4373 O  O   . HOH   I .   ? 0.401 0.325 0.719 0.010  0.022  -0.106 616 HOH   AAA O   
4374 O  O   . HOH   I .   ? 0.765 0.536 0.574 0.133  0.059  0.015  617 HOH   AAA O   
4375 O  O   . HOH   I .   ? 0.524 0.275 0.672 -0.170 0.039  -0.051 618 HOH   AAA O   
4376 O  O   . HOH   I .   ? 0.471 0.112 0.639 -0.056 0.069  -0.014 619 HOH   AAA O   
4377 O  O   . HOH   J .   ? 0.406 0.154 0.478 0.005  -0.006 -0.040 401 HOH   BBB O   
4378 O  O   . HOH   J .   ? 0.499 0.243 0.696 0.056  0.006  -0.026 402 HOH   BBB O   
4379 O  O   . HOH   J .   ? 0.509 0.630 0.925 -0.093 -0.095 0.354  403 HOH   BBB O   
4380 O  O   . HOH   J .   ? 0.534 0.382 0.630 -0.083 -0.008 -0.134 404 HOH   BBB O   
4381 O  O   . HOH   J .   ? 0.618 0.187 0.733 0.067  0.071  0.037  405 HOH   BBB O   
4382 O  O   . HOH   J .   ? 0.376 0.013 0.390 -0.035 -0.072 0.042  406 HOH   BBB O   
4383 O  O   . HOH   J .   ? 0.525 0.316 0.527 -0.146 0.007  -0.090 407 HOH   BBB O   
4384 O  O   . HOH   J .   ? 0.489 0.213 0.620 -0.093 -0.073 -0.002 408 HOH   BBB O   
4385 O  O   . HOH   J .   ? 0.462 0.105 0.504 0.086  0.057  0.018  409 HOH   BBB O   
4386 O  O   . HOH   J .   ? 0.629 0.213 0.628 -0.075 -0.099 -0.038 410 HOH   BBB O   
4387 O  O   . HOH   J .   ? 0.567 0.245 0.593 0.027  0.093  -0.176 411 HOH   BBB O   
4388 O  O   . HOH   J .   ? 0.710 0.543 0.747 0.268  -0.075 -0.166 412 HOH   BBB O   
4389 O  O   . HOH   J .   ? 0.522 0.616 1.178 0.295  0.034  0.299  413 HOH   BBB O   
4390 O  O   . HOH   J .   ? 0.571 0.183 0.577 -0.051 -0.026 0.011  414 HOH   BBB O   
4391 O  O   . HOH   J .   ? 0.425 0.256 0.623 0.090  -0.049 0.089  415 HOH   BBB O   
4392 O  O   . HOH   J .   ? 0.673 0.665 0.435 0.210  0.005  0.030  416 HOH   BBB O   
4393 O  O   . HOH   J .   ? 0.537 0.607 0.505 -0.012 -0.011 -0.029 417 HOH   BBB O   
4394 O  O   . HOH   J .   ? 0.344 0.011 0.507 -0.038 0.004  0.015  418 HOH   BBB O   
4395 O  O   . HOH   J .   ? 0.444 0.304 0.563 0.026  0.057  0.011  419 HOH   BBB O   
4396 O  O   . HOH   J .   ? 0.624 0.103 0.784 -0.048 0.029  -0.027 420 HOH   BBB O   
4397 O  O   . HOH   J .   ? 0.472 0.107 0.498 -0.009 -0.002 -0.010 421 HOH   BBB O   
4398 O  O   . HOH   J .   ? 0.592 0.530 0.739 0.070  -0.156 0.085  422 HOH   BBB O   
4399 O  O   . HOH   J .   ? 0.636 0.353 0.668 0.134  -0.038 0.079  423 HOH   BBB O   
4400 O  O   . HOH   J .   ? 0.827 0.027 0.978 -0.014 0.129  0.133  424 HOH   BBB O   
4401 O  O   . HOH   J .   ? 0.692 0.505 0.637 0.301  -0.039 -0.155 425 HOH   BBB O   
4402 O  O   . HOH   J .   ? 0.548 0.569 0.853 -0.070 0.042  0.155  426 HOH   BBB O   
4403 O  O   . HOH   J .   ? 0.328 0.352 0.487 0.015  0.002  0.064  427 HOH   BBB O   
4404 O  O   . HOH   J .   ? 0.408 0.141 0.490 0.081  -0.029 -0.009 428 HOH   BBB O   
4405 O  O   . HOH   J .   ? 0.478 0.348 0.635 0.203  -0.029 -0.090 429 HOH   BBB O   
4406 O  O   . HOH   J .   ? 0.511 0.152 0.608 -0.032 -0.003 0.060  430 HOH   BBB O   
4407 O  O   . HOH   J .   ? 0.567 0.386 0.733 0.051  0.127  -0.116 431 HOH   BBB O   
4408 O  O   . HOH   J .   ? 0.462 0.047 0.574 -0.039 -0.013 -0.009 432 HOH   BBB O   
4409 O  O   . HOH   J .   ? 0.463 0.167 0.467 -0.089 -0.079 0.104  433 HOH   BBB O   
4410 O  O   . HOH   J .   ? 0.817 0.211 0.658 -0.131 -0.017 -0.037 434 HOH   BBB O   
4411 O  O   . HOH   J .   ? 0.584 0.213 0.660 0.069  -0.026 -0.045 435 HOH   BBB O   
4412 O  O   . HOH   J .   ? 0.458 0.148 0.670 -0.042 0.059  -0.132 436 HOH   BBB O   
4413 O  O   . HOH   J .   ? 0.788 0.179 0.682 -0.064 0.171  0.014  437 HOH   BBB O   
4414 O  O   . HOH   J .   ? 0.561 0.192 0.544 -0.133 0.013  0.087  438 HOH   BBB O   
4415 O  O   . HOH   J .   ? 0.654 0.205 0.686 0.138  0.135  0.044  439 HOH   BBB O   
4416 O  O   . HOH   J .   ? 0.577 0.173 0.540 -0.078 0.035  -0.028 440 HOH   BBB O   
4417 O  O   . HOH   J .   ? 0.547 0.212 0.609 -0.030 -0.010 0.046  441 HOH   BBB O   
4418 O  O   . HOH   J .   ? 0.480 0.274 0.901 -0.045 0.082  0.254  442 HOH   BBB O   
4419 O  O   . HOH   J .   ? 0.694 0.266 0.655 -0.049 0.006  0.075  443 HOH   BBB O   
4420 O  O   . HOH   J .   ? 0.717 0.192 1.128 -0.070 -0.055 0.038  444 HOH   BBB O   
4421 O  O   . HOH   J .   ? 0.415 0.157 0.571 -0.014 -0.017 -0.120 445 HOH   BBB O   
4422 O  O   . HOH   J .   ? 0.490 0.251 0.595 0.038  0.002  -0.073 446 HOH   BBB O   
4423 O  O   . HOH   J .   ? 0.335 0.008 0.425 0.021  0.000  0.013  447 HOH   BBB O   
4424 O  O   . HOH   J .   ? 0.498 0.534 0.545 -0.107 0.002  0.153  448 HOH   BBB O   
4425 O  O   . HOH   J .   ? 0.878 0.407 0.537 -0.219 0.029  0.097  449 HOH   BBB O   
4426 O  O   . HOH   J .   ? 0.598 0.128 0.691 -0.004 -0.026 0.116  450 HOH   BBB O   
4427 O  O   . HOH   J .   ? 0.484 0.127 0.522 -0.092 0.040  -0.063 451 HOH   BBB O   
4428 O  O   . HOH   J .   ? 0.407 0.530 0.686 -0.073 0.129  -0.142 452 HOH   BBB O   
4429 O  O   . HOH   J .   ? 0.327 0.216 0.508 -0.079 0.009  0.068  453 HOH   BBB O   
4430 O  O   . HOH   J .   ? 0.446 0.108 0.625 -0.058 -0.046 -0.135 454 HOH   BBB O   
4431 O  O   . HOH   J .   ? 0.429 0.177 0.588 0.084  0.060  0.084  455 HOH   BBB O   
4432 O  O   . HOH   J .   ? 0.611 0.207 0.922 0.145  -0.038 -0.030 456 HOH   BBB O   
4433 O  O   . HOH   J .   ? 0.464 0.026 0.479 0.003  0.047  0.025  457 HOH   BBB O   
4434 O  O   . HOH   J .   ? 0.662 0.114 0.728 0.012  0.005  0.037  458 HOH   BBB O   
4435 O  O   . HOH   J .   ? 0.457 0.274 0.572 0.100  -0.042 0.098  459 HOH   BBB O   
4436 O  O   . HOH   J .   ? 1.038 0.765 0.853 -0.528 -0.252 0.171  460 HOH   BBB O   
4437 O  O   . HOH   J .   ? 0.362 0.085 0.485 -0.081 -0.013 -0.004 461 HOH   BBB O   
4438 O  O   . HOH   J .   ? 0.351 0.014 0.453 -0.049 0.004  -0.008 462 HOH   BBB O   
4439 O  O   . HOH   J .   ? 0.468 0.464 0.624 -0.035 -0.017 0.123  463 HOH   BBB O   
4440 O  O   . HOH   J .   ? 0.466 0.172 0.687 0.083  -0.016 0.063  464 HOH   BBB O   
4441 O  O   . HOH   J .   ? 0.380 0.136 0.465 0.045  -0.038 0.033  465 HOH   BBB O   
4442 O  O   . HOH   J .   ? 0.879 0.288 0.611 -0.088 0.052  -0.043 466 HOH   BBB O   
4443 O  O   . HOH   J .   ? 0.317 0.179 0.430 0.031  -0.013 -0.052 467 HOH   BBB O   
4444 O  O   . HOH   J .   ? 0.568 0.223 0.602 0.094  0.155  0.055  468 HOH   BBB O   
4445 O  O   . HOH   J .   ? 0.464 0.232 0.535 -0.065 -0.037 0.094  469 HOH   BBB O   
4446 O  O   . HOH   J .   ? 0.332 0.304 0.472 0.011  -0.010 -0.074 470 HOH   BBB O   
4447 O  O   . HOH   J .   ? 0.305 0.045 0.372 0.025  -0.019 0.030  471 HOH   BBB O   
4448 O  O   . HOH   J .   ? 0.305 0.008 0.448 -0.006 0.001  0.028  472 HOH   BBB O   
4449 O  O   . HOH   J .   ? 0.502 0.195 0.604 -0.089 0.059  -0.007 473 HOH   BBB O   
4450 O  O   . HOH   J .   ? 0.371 0.187 0.650 -0.025 -0.019 0.129  474 HOH   BBB O   
4451 O  O   . HOH   J .   ? 0.442 0.200 0.470 0.018  0.004  0.042  475 HOH   BBB O   
4452 O  O   . HOH   J .   ? 0.364 0.235 0.550 0.083  -0.005 0.080  476 HOH   BBB O   
4453 O  O   . HOH   J .   ? 0.552 0.152 0.600 -0.058 0.009  -0.114 477 HOH   BBB O   
4454 O  O   . HOH   J .   ? 0.813 0.228 0.682 -0.072 0.076  -0.120 478 HOH   BBB O   
4455 O  O   . HOH   J .   ? 0.395 0.287 0.521 -0.057 -0.035 0.155  479 HOH   BBB O   
4456 O  O   . HOH   J .   ? 0.454 0.289 0.598 0.163  0.049  0.117  480 HOH   BBB O   
4457 O  O   . HOH   J .   ? 0.572 0.163 0.476 -0.001 0.038  0.088  481 HOH   BBB O   
4458 O  O   . HOH   J .   ? 0.426 0.176 0.600 0.029  0.015  0.055  482 HOH   BBB O   
4459 O  O   . HOH   J .   ? 0.363 0.012 0.526 -0.046 0.013  -0.011 483 HOH   BBB O   
4460 O  O   . HOH   J .   ? 0.561 0.607 0.814 -0.124 0.026  0.228  484 HOH   BBB O   
4461 O  O   . HOH   J .   ? 0.475 0.249 0.729 0.001  -0.088 0.068  485 HOH   BBB O   
4462 O  O   . HOH   J .   ? 0.465 0.091 0.696 0.072  0.035  -0.038 486 HOH   BBB O   
4463 O  O   . HOH   J .   ? 0.486 0.762 0.551 0.114  0.020  0.134  487 HOH   BBB O   
4464 O  O   . HOH   J .   ? 0.509 0.323 0.671 -0.026 0.004  -0.131 488 HOH   BBB O   
4465 O  O   . HOH   J .   ? 0.538 0.116 0.503 -0.037 -0.019 0.003  489 HOH   BBB O   
4466 O  O   . HOH   J .   ? 0.323 0.125 0.456 0.017  -0.042 -0.037 490 HOH   BBB O   
4467 O  O   . HOH   J .   ? 0.511 0.262 0.499 -0.061 0.023  0.037  491 HOH   BBB O   
4468 O  O   . HOH   J .   ? 0.348 0.177 0.417 0.024  0.018  0.010  492 HOH   BBB O   
4469 O  O   . HOH   J .   ? 0.381 0.114 0.604 0.004  -0.092 -0.015 493 HOH   BBB O   
4470 O  O   . HOH   J .   ? 0.682 0.491 0.828 0.235  -0.007 -0.013 494 HOH   BBB O   
4471 O  O   . HOH   J .   ? 0.493 0.264 0.580 0.060  -0.003 -0.139 495 HOH   BBB O   
4472 O  O   . HOH   J .   ? 0.447 0.123 0.435 0.031  -0.041 0.055  496 HOH   BBB O   
4473 O  O   . HOH   J .   ? 0.458 0.316 0.753 0.108  -0.105 -0.130 497 HOH   BBB O   
4474 O  O   . HOH   J .   ? 0.475 0.137 0.616 0.039  0.051  0.027  498 HOH   BBB O   
4475 O  O   . HOH   J .   ? 0.916 0.547 1.023 0.161  0.003  -0.596 499 HOH   BBB O   
4476 O  O   . HOH   J .   ? 0.567 0.075 0.463 0.073  0.078  0.013  500 HOH   BBB O   
4477 O  O   . HOH   J .   ? 0.549 0.144 0.551 0.118  -0.031 0.018  501 HOH   BBB O   
4478 O  O   . HOH   J .   ? 0.632 0.128 0.632 -0.046 -0.125 0.080  502 HOH   BBB O   
4479 O  O   . HOH   J .   ? 0.582 0.086 0.540 0.165  0.022  0.010  503 HOH   BBB O   
4480 O  O   . HOH   J .   ? 0.448 0.007 0.649 0.002  -0.083 -0.023 504 HOH   BBB O   
4481 O  O   . HOH   J .   ? 0.839 0.048 0.749 0.020  -0.094 0.172  505 HOH   BBB O   
4482 O  O   . HOH   J .   ? 0.529 0.198 0.619 0.052  -0.067 0.090  506 HOH   BBB O   
4483 O  O   . HOH   J .   ? 0.602 0.278 0.639 -0.054 0.005  -0.184 507 HOH   BBB O   
4484 O  O   . HOH   J .   ? 0.309 0.272 0.487 0.026  -0.006 -0.072 508 HOH   BBB O   
4485 O  O   . HOH   J .   ? 0.758 0.497 0.672 0.055  0.075  0.136  509 HOH   BBB O   
4486 O  O   . HOH   J .   ? 0.764 0.244 0.699 0.083  0.053  -0.019 510 HOH   BBB O   
4487 O  O   . HOH   J .   ? 0.520 0.254 0.533 0.072  0.008  0.075  511 HOH   BBB O   
4488 O  O   . HOH   J .   ? 0.480 0.109 0.628 0.065  0.086  0.014  512 HOH   BBB O   
4489 O  O   . HOH   J .   ? 0.354 0.009 0.438 0.025  -0.025 -0.018 513 HOH   BBB O   
4490 O  O   . HOH   J .   ? 0.431 0.007 0.518 -0.014 -0.043 -0.001 514 HOH   BBB O   
4491 O  O   . HOH   J .   ? 0.605 0.062 0.638 0.069  0.047  0.007  515 HOH   BBB O   
4492 O  O   . HOH   J .   ? 0.699 0.193 0.503 -0.119 0.015  0.036  516 HOH   BBB O   
4493 O  O   . HOH   J .   ? 0.867 0.311 0.503 0.100  -0.119 0.048  517 HOH   BBB O   
4494 O  O   . HOH   J .   ? 0.465 0.096 0.556 0.032  -0.009 -0.016 518 HOH   BBB O   
4495 O  O   . HOH   J .   ? 0.552 0.147 0.536 -0.149 -0.086 0.123  519 HOH   BBB O   
4496 O  O   . HOH   J .   ? 0.731 0.360 0.623 -0.194 -0.220 0.144  520 HOH   BBB O   
4497 O  O   . HOH   J .   ? 0.667 0.008 0.506 -0.032 -0.010 0.010  521 HOH   BBB O   
4498 O  O   . HOH   J .   ? 0.543 0.286 0.640 -0.004 0.033  0.241  522 HOH   BBB O   
4499 O  O   . HOH   J .   ? 0.742 0.229 0.697 0.044  0.253  0.016  523 HOH   BBB O   
4500 O  O   . HOH   J .   ? 0.591 0.030 0.685 -0.012 0.016  0.003  524 HOH   BBB O   
4501 O  O   . HOH   J .   ? 0.577 0.140 0.571 0.005  0.056  -0.003 525 HOH   BBB O   
4502 O  O   . HOH   J .   ? 0.524 0.399 0.605 0.197  0.122  0.104  526 HOH   BBB O   
4503 O  O   . HOH   J .   ? 0.535 0.435 0.596 -0.176 0.015  -0.185 527 HOH   BBB O   
4504 O  O   . HOH   J .   ? 0.561 0.478 0.642 0.237  -0.029 0.037  528 HOH   BBB O   
4505 O  O   . HOH   J .   ? 0.487 0.278 0.572 -0.043 -0.068 0.007  529 HOH   BBB O   
4506 O  O   . HOH   J .   ? 0.339 0.118 0.489 0.033  -0.002 0.046  530 HOH   BBB O   
4507 O  O   . HOH   J .   ? 0.663 0.261 0.555 0.158  0.029  0.089  531 HOH   BBB O   
4508 O  O   . HOH   J .   ? 0.443 0.128 0.624 -0.046 -0.059 0.054  532 HOH   BBB O   
4509 O  O   . HOH   J .   ? 0.408 0.104 0.698 0.029  -0.108 -0.052 533 HOH   BBB O   
4510 O  O   . HOH   J .   ? 0.554 0.500 0.653 0.032  0.081  -0.151 534 HOH   BBB O   
4511 O  O   . HOH   J .   ? 0.467 0.347 0.600 -0.025 0.024  0.079  535 HOH   BBB O   
4512 O  O   . HOH   J .   ? 0.334 0.009 0.409 -0.007 0.021  0.031  536 HOH   BBB O   
4513 O  O   . HOH   J .   ? 0.935 0.634 0.577 0.250  0.130  0.121  537 HOH   BBB O   
4514 O  O   . HOH   J .   ? 0.695 0.537 0.617 -0.126 -0.127 0.090  538 HOH   BBB O   
4515 O  O   . HOH   J .   ? 0.351 0.022 0.471 0.051  -0.027 -0.067 539 HOH   BBB O   
4516 O  O   . HOH   J .   ? 0.436 0.243 0.550 -0.022 -0.015 0.041  540 HOH   BBB O   
4517 O  O   . HOH   J .   ? 0.675 0.213 0.743 0.028  -0.034 0.002  541 HOH   BBB O   
4518 O  O   . HOH   J .   ? 0.576 0.119 0.627 0.143  -0.044 0.026  542 HOH   BBB O   
4519 O  O   . HOH   J .   ? 0.474 0.256 0.579 -0.119 0.012  -0.101 543 HOH   BBB O   
4520 O  O   . HOH   J .   ? 0.505 0.351 0.950 -0.076 0.017  0.191  544 HOH   BBB O   
4521 O  O   . HOH   J .   ? 0.560 0.319 0.613 0.050  0.032  0.021  545 HOH   BBB O   
4522 O  O   . HOH   J .   ? 0.551 0.380 0.807 0.014  -0.082 -0.094 546 HOH   BBB O   
4523 O  O   . HOH   J .   ? 0.661 0.282 0.624 0.212  0.109  0.071  547 HOH   BBB O   
4524 O  O   . HOH   J .   ? 0.321 0.009 0.440 -0.005 -0.021 -0.036 548 HOH   BBB O   
4525 O  O   . HOH   J .   ? 0.385 0.132 0.412 0.021  0.023  -0.057 549 HOH   BBB O   
4526 O  O   . HOH   J .   ? 0.652 0.543 0.610 -0.129 -0.062 0.067  550 HOH   BBB O   
4527 O  O   . HOH   J .   ? 0.678 0.675 0.759 -0.171 0.109  0.023  551 HOH   BBB O   
4528 O  O   . HOH   J .   ? 0.678 0.085 0.634 -0.026 -0.093 0.090  552 HOH   BBB O   
4529 O  O   . HOH   J .   ? 0.561 0.139 0.602 0.025  -0.007 -0.007 553 HOH   BBB O   
4530 O  O   . HOH   J .   ? 0.699 0.210 0.718 0.076  0.063  -0.054 554 HOH   BBB O   
4531 O  O   . HOH   J .   ? 0.452 0.049 0.510 -0.027 0.029  0.047  555 HOH   BBB O   
4532 O  O   . HOH   J .   ? 0.428 0.498 0.436 0.227  -0.054 -0.032 556 HOH   BBB O   
4533 O  O   . HOH   J .   ? 0.499 0.088 0.816 -0.042 0.084  -0.135 557 HOH   BBB O   
4534 O  O   . HOH   J .   ? 0.847 0.094 0.603 0.042  0.068  0.013  558 HOH   BBB O   
4535 O  O   . HOH   J .   ? 0.588 0.201 0.478 0.154  0.040  0.054  559 HOH   BBB O   
4536 O  O   . HOH   J .   ? 0.368 0.277 0.652 -0.053 -0.076 0.137  560 HOH   BBB O   
4537 O  O   . HOH   J .   ? 0.821 0.592 0.759 -0.237 0.153  -0.207 561 HOH   BBB O   
4538 O  O   . HOH   J .   ? 0.603 0.299 0.671 0.004  0.015  0.038  562 HOH   BBB O   
4539 O  O   . HOH   J .   ? 0.412 0.175 0.588 0.072  -0.005 0.135  563 HOH   BBB O   
4540 O  O   . HOH   J .   ? 0.367 0.165 0.559 0.067  -0.014 -0.108 564 HOH   BBB O   
4541 O  O   . HOH   J .   ? 0.515 0.455 0.550 -0.195 -0.059 0.120  565 HOH   BBB O   
4542 O  O   . HOH   J .   ? 0.529 0.258 0.734 -0.055 0.101  -0.030 566 HOH   BBB O   
4543 O  O   . HOH   J .   ? 0.360 0.141 0.446 0.013  0.015  -0.001 567 HOH   BBB O   
4544 O  O   . HOH   J .   ? 0.551 0.152 0.499 -0.079 0.043  -0.016 568 HOH   BBB O   
4545 O  O   . HOH   J .   ? 0.594 0.230 0.390 -0.027 -0.054 0.033  569 HOH   BBB O   
4546 O  O   . HOH   J .   ? 0.468 0.199 0.728 -0.250 0.162  -0.223 570 HOH   BBB O   
4547 O  O   . HOH   J .   ? 0.476 0.310 0.615 0.044  -0.025 -0.130 571 HOH   BBB O   
4548 O  O   . HOH   J .   ? 0.512 0.185 0.579 0.053  0.150  0.058  572 HOH   BBB O   
4549 O  O   . HOH   J .   ? 0.600 0.468 0.718 0.145  -0.022 -0.145 573 HOH   BBB O   
4550 O  O   . HOH   J .   ? 0.841 0.386 0.715 -0.141 -0.150 -0.011 574 HOH   BBB O   
4551 O  O   . HOH   J .   ? 0.662 0.238 0.882 -0.045 0.187  0.106  575 HOH   BBB O   
4552 O  O   . HOH   J .   ? 0.980 0.306 0.698 0.134  -0.036 -0.017 576 HOH   BBB O   
4553 O  O   . HOH   J .   ? 0.680 0.369 0.657 0.106  0.065  -0.034 577 HOH   BBB O   
4554 O  O   . HOH   J .   ? 0.987 0.441 0.675 -0.122 -0.173 -0.062 578 HOH   BBB O   
4555 O  O   . HOH   J .   ? 0.558 0.224 0.596 -0.018 0.056  0.007  579 HOH   BBB O   
4556 O  O   . HOH   J .   ? 0.460 0.215 0.676 0.044  0.094  0.019  580 HOH   BBB O   
4557 O  O   . HOH   J .   ? 0.463 0.935 0.543 0.170  -0.076 -0.157 581 HOH   BBB O   
4558 O  O   . HOH   J .   ? 0.778 0.158 0.732 -0.233 0.004  -0.052 582 HOH   BBB O   
4559 O  O   . HOH   J .   ? 0.730 0.823 0.616 -0.011 0.147  0.194  583 HOH   BBB O   
4560 O  O   . HOH   J .   ? 1.131 0.334 0.635 0.043  -0.158 0.042  584 HOH   BBB O   
4561 O  O   . HOH   J .   ? 0.573 0.343 0.526 0.138  0.057  0.012  585 HOH   BBB O   
4562 O  O   . HOH   J .   ? 0.509 0.242 0.579 0.100  -0.104 -0.073 586 HOH   BBB O   
4563 O  O   . HOH   J .   ? 0.487 0.332 0.947 -0.031 -0.000 0.105  587 HOH   BBB O   
4564 O  O   . HOH   J .   ? 0.734 0.349 0.678 -0.006 -0.070 0.173  588 HOH   BBB O   
4565 O  O   . HOH   J .   ? 0.956 0.183 0.568 0.033  0.030  0.017  589 HOH   BBB O   
4566 O  O   . HOH   J .   ? 0.631 0.320 1.010 -0.047 0.031  -0.046 590 HOH   BBB O   
4567 O  O   . HOH   J .   ? 0.832 0.312 1.158 0.007  -0.152 -0.018 591 HOH   BBB O   
4568 O  O   . HOH   J .   ? 0.402 0.006 0.540 -0.003 0.043  -0.001 592 HOH   BBB O   
4569 O  O   . HOH   J .   ? 0.690 0.263 0.604 0.186  -0.044 -0.016 593 HOH   BBB O   
4570 O  O   . HOH   J .   ? 0.556 0.239 0.661 -0.048 0.070  -0.143 594 HOH   BBB O   
4571 O  O   . HOH   J .   ? 0.773 0.227 0.629 0.206  -0.095 0.012  595 HOH   BBB O   
4572 O  O   . HOH   J .   ? 0.444 0.275 0.487 0.034  -0.068 0.119  596 HOH   BBB O   
4573 O  O   . HOH   J .   ? 0.639 0.231 0.564 0.032  0.054  -0.003 597 HOH   BBB O   
4574 O  O   . HOH   J .   ? 0.368 0.258 0.834 -0.006 0.056  -0.149 598 HOH   BBB O   
4575 O  O   . HOH   J .   ? 0.411 0.302 0.476 0.018  0.005  0.026  599 HOH   BBB O   
4576 O  O   . HOH   J .   ? 0.591 0.287 0.844 0.102  -0.077 -0.138 600 HOH   BBB O   
4577 O  O   . HOH   J .   ? 0.412 0.170 0.452 0.091  -0.040 -0.044 601 HOH   BBB O   
4578 O  O   . HOH   J .   ? 0.499 0.170 0.565 -0.006 0.015  -0.041 602 HOH   BBB O   
4579 O  O   . HOH   J .   ? 0.759 0.233 0.615 -0.106 0.063  0.022  603 HOH   BBB O   
4580 O  O   . HOH   J .   ? 0.528 0.784 0.754 0.014  -0.124 0.048  604 HOH   BBB O   
4581 O  O   . HOH   J .   ? 0.328 0.111 0.466 0.021  -0.042 -0.020 605 HOH   BBB O   
4582 O  O   . HOH   J .   ? 0.480 0.320 0.903 0.019  -0.050 -0.103 606 HOH   BBB O   
4583 O  O   . HOH   J .   ? 0.467 0.437 0.591 0.093  0.072  0.078  607 HOH   BBB O   
4584 O  O   . HOH   J .   ? 0.631 0.504 0.675 -0.225 0.084  0.116  608 HOH   BBB O   
4585 O  O   . HOH   J .   ? 0.708 0.301 0.750 0.058  0.116  0.080  609 HOH   BBB O   
4586 O  O   . HOH   J .   ? 0.523 0.292 1.144 0.011  -0.044 -0.050 610 HOH   BBB O   
4587 O  O   . HOH   J .   ? 0.588 0.213 0.679 0.055  -0.001 -0.166 611 HOH   BBB O   
4588 O  O   . HOH   J .   ? 0.533 0.362 0.510 -0.002 -0.004 0.120  612 HOH   BBB O   
4589 O  O   . HOH   J .   ? 0.710 0.608 0.790 -0.027 -0.235 0.158  613 HOH   BBB O   
4590 O  O   . HOH   J .   ? 0.508 0.429 0.634 0.139  -0.001 -0.043 614 HOH   BBB O   
4591 O  O   . HOH   J .   ? 0.541 0.205 0.633 -0.047 0.040  -0.073 615 HOH   BBB O   
4592 O  O   . HOH   J .   ? 0.637 0.305 0.605 0.057  0.022  -0.006 616 HOH   BBB O   
4593 O  O   . HOH   J .   ? 0.567 0.119 0.709 0.045  0.072  -0.042 617 HOH   BBB O   
4594 O  O   . HOH   J .   ? 0.601 0.525 0.605 0.062  -0.037 0.085  618 HOH   BBB O   
4595 O  O   . HOH   J .   ? 0.716 0.287 0.505 -0.141 -0.065 0.075  619 HOH   BBB O   
4596 O  O   . HOH   J .   ? 0.435 0.103 0.640 0.012  -0.068 0.079  620 HOH   BBB O   
4597 O  O   . HOH   J .   ? 0.474 0.563 0.646 0.166  0.008  0.070  621 HOH   BBB O   
4598 O  O   . HOH   J .   ? 0.765 0.200 0.655 0.025  0.138  0.013  622 HOH   BBB O   
4599 O  O   . HOH   J .   ? 0.987 0.491 0.444 -0.341 -0.092 0.066  623 HOH   BBB O   
# 
